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This is a searchable collection of scientific photos, illustrations, and videos. The images and videos in this gallery are licensed under Creative Commons Attribution Non-Commercial ShareAlike 3.0. This license lets you remix, tweak, and build upon this work non-commercially, as long as you credit and license your new creations under identical terms.
3446: Biofilm blocking fluid flow
3446: Biofilm blocking fluid flow
This time-lapse movie shows that bacterial communities called biofilms can create blockages that prevent fluid flow in devices such as stents and catheters over a period of about 56 hours. This video was featured in a news release from Princeton University.
Bonnie Bassler, Princeton University
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6791: Yeast cells entering mitosis
6791: Yeast cells entering mitosis
Yeast cells entering mitosis, also known as cell division. The green and magenta dots are two proteins that play important roles in mitosis. They show where the cells will split. This image was captured using wide-field microscopy with deconvolution.
Related to images 6792, 6793, 6794, 6797, 6798, and videos 6795 and 6796.
Related to images 6792, 6793, 6794, 6797, 6798, and videos 6795 and 6796.
Alaina Willet, Kathy Gould’s lab, Vanderbilt University.
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3610: Human liver cell (hepatocyte)
3610: Human liver cell (hepatocyte)
Hepatocytes, like the one shown here, are the most abundant type of cell in the human liver. They play an important role in building proteins; producing bile, a liquid that aids in digesting fats; and chemically processing molecules found normally in the body, like hormones, as well as foreign substances like medicines and alcohol.
This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.
This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.
Donna Beer Stolz, University of Pittsburgh
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6344: Drosophila
6344: Drosophila
Two adult fruit flies (Drosophila)
Dr. Vicki Losick, MDI Biological Laboratory, www.mdibl.org
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2388: Ubiquitin-fold modifier 1 from C. elegans
2388: Ubiquitin-fold modifier 1 from C. elegans
Solution NMR structure of protein target WR41 (left) from C. elegans. Noting the unanticipated structural similarity to the ubiquitin protein (Ub) found in all eukaryotic cells, researchers discovered that WR41 is a Ub-like modifier, ubiquitin-fold modifier 1 (Ufm1), on a newly uncovered ubiquitin-like pathway. Subsequently, the PSI group also determined the three-dimensional structure of protein target HR41 (right) from humans, the E2 ligase for Ufm1, using both NMR and X-ray crystallography.
Northeast Structural Genomics Consortium
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1310: Cell cycle wheel
1310: Cell cycle wheel
A typical animal cell cycle lasts roughly 24 hours, but depending on the type of cell, it can vary in length from less than 8 hours to more than a year. Most of the variability occurs in Gap1. Appears in the NIGMS booklet Inside the Cell.
Judith Stoffer
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2526: Activation energy (with labels)
2526: Activation energy (with labels)
To become products, reactants must overcome an energy hill. See image 2525 for an unlabeled version of this illustration. Featured in The Chemistry of Health.
Crabtree + Company
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3417: X-ray co-crystal structure of Src kinase bound to a DNA-templated macrocycle inhibitor 5
3417: X-ray co-crystal structure of Src kinase bound to a DNA-templated macrocycle inhibitor 5
X-ray co-crystal structure of Src kinase bound to a DNA-templated macrocycle inhibitor. Related to images 3413, 3414, 3415, 3416, 3418, and 3419.
Markus A. Seeliger, Stony Brook University Medical School and David R. Liu, Harvard University
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1157: Streptococcus bacteria
1157: Streptococcus bacteria
Image of Streptococcus, a type (genus) of spherical bacteria that can colonize the throat and back of the mouth. Stroptococci often occur in pairs or in chains, as shown here.
Tina Weatherby Carvalho, University of Hawaii at Manoa
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2607: Mouse embryo showing Smad4 protein
2607: Mouse embryo showing Smad4 protein
This eerily glowing blob isn't an alien or a creature from the deep sea--it's a mouse embryo just eight and a half days old. The green shell and core show a protein called Smad4. In the center, Smad4 is telling certain cells to begin forming the mouse's liver and pancreas. Researchers identified a trio of signaling pathways that help switch on Smad4-making genes, starting immature cells on the path to becoming organs. The research could help biologists learn how to grow human liver and pancreas tissue for research, drug testing and regenerative medicine. In addition to NIGMS, NIH's National Institute of Diabetes and Digestive and Kidney Diseases also supported this work.
Kenneth Zaret, Fox Chase Cancer Center
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2551: Introns (with labels)
2551: Introns (with labels)
Genes are often interrupted by stretches of DNA (introns, blue) that do not contain instructions for making a protein. The DNA segments that do contain protein-making instructions are known as exons (green). See image 2550 for an unlabeled version of this illustration. Featured in The New Genetics.
Crabtree + Company
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2426: Zinc finger
2426: Zinc finger
The structure of a gene-regulating zinc finger protein bound to DNA.
Jeremy M. Berg, National Institute of General Medical Sciences
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5877: Misfolded proteins in mitochondria, 3-D video
5877: Misfolded proteins in mitochondria, 3-D video
Three-dimensional image of misfolded proteins (green) within mitochondria (red). Related to image 5878. Learn more in this press release by The American Association for the Advancement of Science.
Rong Li, Department of Chemical and Biomolecular Engineering, Whiting School of Engineering, Johns Hopkins University
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3787: In vitro assembly of a cell-signaling pathway
3787: In vitro assembly of a cell-signaling pathway
T cells are white blood cells that are important in defending the body against bacteria, viruses and other pathogens. Each T cell carries proteins, called T-cell receptors, on its surface that are activated when they come in contact with an invader. This activation sets in motion a cascade of biochemical changes inside the T cell to mount a defense against the invasion. Scientists have been interested for some time what happens after a T-cell receptor is activated. One obstacle has been to study how this signaling cascade, or pathway, proceeds inside T cells.
In this image, researchers have created a T-cell receptor pathway consisting of 12 proteins outside the cell on an artificial membrane. The image shows two key steps during the signaling process: clustering of a protein called linker for activation of T cells (LAT) (blue) and polymerization of the cytoskeleton protein actin (red). The findings show that the T-cell receptor signaling proteins self-organize into separate physical and biochemical compartments. This new system of studying molecular pathways outside the cells will enable scientists to better understand how the immune system combats microbes or other agents that cause infection.
To learn more how researchers assembled this T-cell receptor pathway, see this press release from HHMI's Marine Biological Laboratory Whitman Center. Related to video 3786.
In this image, researchers have created a T-cell receptor pathway consisting of 12 proteins outside the cell on an artificial membrane. The image shows two key steps during the signaling process: clustering of a protein called linker for activation of T cells (LAT) (blue) and polymerization of the cytoskeleton protein actin (red). The findings show that the T-cell receptor signaling proteins self-organize into separate physical and biochemical compartments. This new system of studying molecular pathways outside the cells will enable scientists to better understand how the immune system combats microbes or other agents that cause infection.
To learn more how researchers assembled this T-cell receptor pathway, see this press release from HHMI's Marine Biological Laboratory Whitman Center. Related to video 3786.
Xiaolei Su, HHMI Whitman Center of the Marine Biological Laboratory
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6581: Fluorescent C. elegans showing muscle and ribosomal protein
6581: Fluorescent C. elegans showing muscle and ribosomal protein
C. elegans, a tiny roundworm, with a ribosomal protein glowing red and muscle fibers glowing green. Researchers used these worms to study a molecular pathway that affects aging. The ribosomal protein is involved in protein translation and may play a role in dietary restriction-induced longevity. Image created using confocal microscopy.
View group of roundworms here 6582.
View closeup of roundworms here 6583.
View group of roundworms here 6582.
View closeup of roundworms here 6583.
Jarod Rollins, Mount Desert Island Biological Laboratory.
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3598: Developing zebrafish fin
3598: Developing zebrafish fin
Originally from the waters of India, Nepal, and neighboring countries, zebrafish can now be found swimming in science labs (and home aquariums) throughout the world. This fish is a favorite study subject for scientists interested in how genes guide the early stages of prenatal development (including the developing fin shown here) and in the effects of environmental contamination on embryos.
In this image, green fluorescent protein (GFP) is expressed where the gene sox9b is expressed. Collagen (red) marks the fin rays, and DNA, stained with a dye called DAPI, is in blue. sox9b plays many important roles during development, including the building of the heart and brain, and is also necessary for skeletal development. At the University of Wisconsin, researchers have found that exposure to contaminants that bind the aryl-hydrocarbon receptor results in the downregulation of sox9b. Loss of sox9b severely disrupts development in zebrafish and causes a life-threatening disorder called campomelic dysplasia (CD) in humans. CD is characterized by cardiovascular, neural, and skeletal defects. By studying the roles of genes such as sox9b in zebrafish, scientists hope to better understand normal development in humans as well as how to treat developmental disorders and diseases.
This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.
In this image, green fluorescent protein (GFP) is expressed where the gene sox9b is expressed. Collagen (red) marks the fin rays, and DNA, stained with a dye called DAPI, is in blue. sox9b plays many important roles during development, including the building of the heart and brain, and is also necessary for skeletal development. At the University of Wisconsin, researchers have found that exposure to contaminants that bind the aryl-hydrocarbon receptor results in the downregulation of sox9b. Loss of sox9b severely disrupts development in zebrafish and causes a life-threatening disorder called campomelic dysplasia (CD) in humans. CD is characterized by cardiovascular, neural, and skeletal defects. By studying the roles of genes such as sox9b in zebrafish, scientists hope to better understand normal development in humans as well as how to treat developmental disorders and diseases.
This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.
Jessica Plavicki
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3365: Chemokine CXCR4 receptor
3365: Chemokine CXCR4 receptor
The receptor is shown bound to a small molecule peptide called CVX15.
Raymond Stevens, The Scripps Research Institute
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2534: Kinases
2534: Kinases
Kinases are enzymes that add phosphate groups (red-yellow structures) to proteins (green), assigning the proteins a code. In this reaction, an intermediate molecule called ATP (adenosine triphosphate) donates a phosphate group from itself, becoming ADP (adenosine diphosphate). See image 2535 for a labeled version of this illustration. Featured in Medicines By Design.
Crabtree + Company
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6765: X-ray diffraction pattern from a crystallized cefotaxime-CCD-1 complex
6765: X-ray diffraction pattern from a crystallized cefotaxime-CCD-1 complex
CCD-1 is an enzyme produced by the bacterium Clostridioides difficile that helps it resist antibiotics. Researchers crystallized complexes where a CCD-1 molecule and a molecule of the antibiotic cefotaxime were bound together. Then, they shot X-rays at the complexes to determine their structure—a process known as X-ray crystallography. This image shows the X-ray diffraction pattern of a complex.
Related to images 6764, 6766, and 6767.
Related to images 6764, 6766, and 6767.
Keith Hodgson, Stanford University.
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6777: Human endoplasmic reticulum membrane protein complex
6777: Human endoplasmic reticulum membrane protein complex
A 3D model of the human endoplasmic reticulum membrane protein complex (EMC) that identifies its nine essential subunits. The EMC plays an important role in making membrane proteins, which are essential for all cellular processes. This is the first atomic-level depiction of the EMC. Its structure was obtained using single-particle cryo-electron microscopy.
Rebecca Voorhees, California Institute of Technology.
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1191: Mouse sperm sections
1191: Mouse sperm sections
This transmission electron micrograph shows sections of mouse sperm tails, or flagella.
Tina Weatherby Carvalho, University of Hawaii at Manoa
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3521: HeLa cells
3521: HeLa cells
Multiphoton fluorescence image of HeLa cells stained with the actin binding toxin phalloidin (red), microtubules (cyan) and cell nuclei (blue). Nikon RTS2000MP custom laser scanning microscope. See related images 3518, 3519, 3520, 3522.
National Center for Microscopy and Imaging Research (NCMIR)
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6794: Yeast cells with Fimbrin Fim1
6794: Yeast cells with Fimbrin Fim1
Yeast cells with the protein Fimbrin Fim1 shown in magenta. This protein plays a role in cell division. This image was captured using wide-field microscopy with deconvolution.
Related to images 6791, 6792, 6793, 6797, 6798, and videos 6795 and 6796.
Related to images 6791, 6792, 6793, 6797, 6798, and videos 6795 and 6796.
Alaina Willet, Kathy Gould’s lab, Vanderbilt University.
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2596: Sleep and the fly brain
2596: Sleep and the fly brain
In the top snapshots, the brain of a sleep-deprived fruit fly glows orange, marking high concentrations of a synaptic protein called Bruchpilot (BRP) involved in communication between neurons. The color particularly lights up brain areas associated with learning. By contrast, the bottom images from a well-rested fly show lower levels of the protein. These pictures illustrate the results of an April 2009 study showing that sleep reduces the protein's levels, suggesting that such "downscaling" resets the brain to normal levels of synaptic activity and makes it ready to learn after a restful night.
Chiara Cirelli, University of Wisconsin-Madison
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3756: Protective membrane and membrane proteins of the dengue virus visualized with cryo-EM
3756: Protective membrane and membrane proteins of the dengue virus visualized with cryo-EM
Dengue virus is a mosquito-borne illness that infects millions of people in the tropics and subtropics each year. Like many viruses, dengue is enclosed by a protective membrane. The proteins that span this membrane play an important role in the life cycle of the virus. Scientists used cryo-EM to determine the structure of a dengue virus at a 3.5-angstrom resolution to reveal how the membrane proteins undergo major structural changes as the virus matures and infects a host. For more on cryo-EM see the blog post Cryo-Electron Microscopy Reveals Molecules in Ever Greater Detail. You can watch a rotating view of the dengue virus surface structure in video 3748.
Hong Zhou, UCLA
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3745: Serum albumin structure 2
3745: Serum albumin structure 2
Serum albumin (SA) is the most abundant protein in the blood plasma of mammals. SA has a characteristic heart-shape structure and is a highly versatile protein. It helps maintain normal water levels in our tissues and carries almost half of all calcium ions in human blood. SA also transports some hormones, nutrients and metals throughout the bloodstream. Despite being very similar to our own SA, those from other animals can cause some mild allergies in people. Therefore, some scientists study SAs from humans and other mammals to learn more about what subtle structural or other differences cause immune responses in the body.
Related to entries 3744 and 3746
Related to entries 3744 and 3746
Wladek Minor, University of Virginia
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2434: Fruit fly retina 02
2434: Fruit fly retina 02
Section of a fruit fly retina showing the light-sensing molecules rhodopsin-5 (blue) and rhodopsin-6 (red).
Hermann Steller, Rockefeller University
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1312: Cell toxins
1312: Cell toxins
A number of environmental factors cause DNA mutations that can lead to cancer: toxins in cigarette smoke, sunlight and other radiation, and some viruses.
Judith Stoffer
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3793: Nucleolus subcompartments spontaneously self-assemble 4
3793: Nucleolus subcompartments spontaneously self-assemble 4
What looks a little like distant planets with some mysterious surface features are actually assemblies of proteins normally found in the cell's nucleolus, a small but very important protein complex located in the cell's nucleus. It forms on the chromosomes at the location where the genes for the RNAs are that make up the structure of the ribosome, the indispensable cellular machine that makes proteins from messenger RNAs.
However, how the nucleolus grows and maintains its structure has puzzled scientists for some time. It turns out that even though it looks like a simple liquid blob, it's rather well-organized, consisting of three distinct layers: the fibrillar center, where the RNA polymerase is active; the dense fibrillar component, which is enriched in the protein fibrillarin; and the granular component, which contains a protein called nucleophosmin. Researchers have now discovered that this multilayer structure of the nucleolus arises from differences in how the proteins in each compartment mix with water and with each other. These differences let the proteins readily separate from each other into the three nucleolus compartments.
This photo of nucleolus proteins in the eggs of a commonly used lab animal, the frog Xenopus laevis, shows each of the nucleolus compartments (the granular component is shown in red, the fibrillarin in yellow-green, and the fibrillar center in blue). The researchers have found that these compartments spontaneously fuse with each other on encounter without mixing with the other compartments.
For more details on this research, see this press release from Princeton. Related to video 3789, video 3791 and image 3792.
However, how the nucleolus grows and maintains its structure has puzzled scientists for some time. It turns out that even though it looks like a simple liquid blob, it's rather well-organized, consisting of three distinct layers: the fibrillar center, where the RNA polymerase is active; the dense fibrillar component, which is enriched in the protein fibrillarin; and the granular component, which contains a protein called nucleophosmin. Researchers have now discovered that this multilayer structure of the nucleolus arises from differences in how the proteins in each compartment mix with water and with each other. These differences let the proteins readily separate from each other into the three nucleolus compartments.
This photo of nucleolus proteins in the eggs of a commonly used lab animal, the frog Xenopus laevis, shows each of the nucleolus compartments (the granular component is shown in red, the fibrillarin in yellow-green, and the fibrillar center in blue). The researchers have found that these compartments spontaneously fuse with each other on encounter without mixing with the other compartments.
For more details on this research, see this press release from Princeton. Related to video 3789, video 3791 and image 3792.
Nilesh Vaidya, Princeton University
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3427: Antitoxin GhoS (Illustration 1)
3427: Antitoxin GhoS (Illustration 1)
Structure of the bacterial antitoxin protein GhoS. GhoS inhibits the production of a bacterial toxin, GhoT, which can contribute to antibiotic resistance. GhoS is the first known bacterial antitoxin that works by cleaving the messenger RNA that carries the instructions for making the toxin. More information can be found in the paper: Wang X, Lord DM, Cheng HY, Osbourne DO, Hong SH, Sanchez-Torres V, Quiroga C, Zheng K, Herrmann T, Peti W, Benedik MJ, Page R, Wood TK. A new type V toxin-antitoxin system where mRNA for toxin GhoT is cleaved by antitoxin GhoS. Nat Chem Biol. 2012 Oct;8(10):855-61. Related to 3428.
Rebecca Page and Wolfgang Peti, Brown University and Thomas K. Wood, Pennsylvania State University
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2320: Mapping disease spread
2320: Mapping disease spread
How far and fast an infectious disease spreads across a community depends on many factors, including transportation. These U.S. maps, developed as part of an international study to simulate and analyze disease spread, chart daily commuting patterns. They show where commuters live (top) and where they travel for work (bottom). Green represents the fewest number of people whereas orange, brown, and white depict the most. Such information enables researchers and policymakers to visualize how an outbreak in one area can spread quickly across a geographic region.
David Chrest, RTI International
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2372: Wreath-shaped protein from X. campestris
2372: Wreath-shaped protein from X. campestris
Crystal structure of a protein with unknown function from Xanthomonas campestris, a plant pathogen. Eight copies of the protein crystallized to form a ring. Chosen as the December 2007 Protein Structure Initiative Structure of the Month.
Ken Schwinn and Sonia Espejon-Reynes, New York SGX Research Center for Structural Genomics
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3687: Hippocampal neuron in culture
3687: Hippocampal neuron in culture
Hippocampal neuron in culture. Dendrites are green, dendritic spines are red and DNA in cell's nucleus is blue. Image is featured on Biomedical Beat blog post Anesthesia and Brain Cells: A Temporary Disruption?
Shelley Halpain, UC San Diego
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3660: Ribonuclease P structure
3660: Ribonuclease P structure
Ribbon diagram showing the structure of Ribonuclease P with tRNA.
PDB entry 3Q1Q, molecular modeling by Fred Friedman, NIGMS
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6602: See how immune cell acid destroys bacterial proteins
6602: See how immune cell acid destroys bacterial proteins
This animation shows the effect of exposure to hypochlorous acid, which is found in certain types of immune cells, on bacterial proteins. The proteins unfold and stick to one another, leading to cell death.
American Chemistry Council
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3766: TFIID complex binds DNA to start gene transcription
3766: TFIID complex binds DNA to start gene transcription
Gene transcription is a process by which the genetic information encoded in DNA is transcribed into RNA. It's essential for all life and requires the activity of proteins, called transcription factors, that detect where in a DNA strand transcription should start. In eukaryotes (i.e., those that have a nucleus and mitochondria), a protein complex comprising 14 different proteins is responsible for sniffing out transcription start sites and starting the process. This complex, called TFIID, represents the core machinery to which an enzyme, named RNA polymerase, can bind to and read the DNA and transcribe it to RNA. Scientists have used cryo-electron microscopy (cryo-EM) to visualize the TFIID-RNA polymerase-DNA complex in unprecedented detail. In this illustration, TFIID (blue) contacts the DNA and recruits the RNA polymerase (gray) for gene transcription. The start of the transcribed gene is shown with a flash of light. To learn more about the research that has shed new light on gene transcription, see this news release from Berkeley Lab. Related to video 5730.
Eva Nogales, Berkeley Lab
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2518: ATP synthase (with labels)
2518: ATP synthase (with labels)
The world's smallest motor, ATP synthase, generates energy for the cell. See image 2517 for an unlabeled version of this illustration. Featured in The Chemistry of Health.
Crabtree + Company
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6780: Calling Cards in a mouse brain
6780: Calling Cards in a mouse brain
The green spots in this mouse brain are cells labeled with Calling Cards, a technology that records molecular events in brain cells as they mature. Understanding these processes during healthy development can guide further research into what goes wrong in cases of neuropsychiatric disorders. Also fluorescently labeled in this image are neurons (red) and nuclei (blue). Calling Cards and its application are described in the Cell paper “Self-Reporting Transposons Enable Simultaneous Readout of Gene Expression and Transcription Factor Binding in Single Cells” by Moudgil et al.; and the Proceedings of the National Academy of Sciences paper “A viral toolkit for recording transcription factor–DNA interactions in live mouse tissues” by Cammack et al. The technology was also featured in the NIH Director’s Blog post The Amazing Brain: Tracking Molecular Events with Calling Cards.
Related to video
Related to video
Allen Yen, Lab of Joseph Dougherty, Washington University School of Medicine in St. Louis.
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7020: Bacterial symbionts colonizing the crypts of a juvenile Hawaiian bobtail squid light organ
7020: Bacterial symbionts colonizing the crypts of a juvenile Hawaiian bobtail squid light organ
A light organ (~0.5 mm across) of a Hawaiian bobtail squid, Euprymna scolopes, stained blue. At the time of this image, the crypts within the tissues of only one side of the organ had been colonized by green-fluorescent protein-labeled Vibrio fischeri cells, which can be seen here in green. This image was taken using confocal fluorescence microscopy.
Related to images 7016, 7017, 7018, and 7019.
Related to images 7016, 7017, 7018, and 7019.
Margaret J. McFall-Ngai, Carnegie Institution for Science/California Institute of Technology, and Edward G. Ruby, California Institute of Technology.
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2357: Capillary protein crystallization robot
2357: Capillary protein crystallization robot
This ACAPELLA robot for capillary protein crystallization grows protein crystals, freezes them, and centers them without manual intervention. The close-up is a view of one of the dispensers used for dispensing proteins and reagents.
Structural Genomics of Pathogenic Protozoa Consortium
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5843: Color coding of the Drosophila brain - video
5843: Color coding of the Drosophila brain - video
This video results from a research project to visualize which regions of the adult fruit fly (Drosophila) brain derive from each neural stem cell. First, researchers collected several thousand fruit fly larvae and fluorescently stained a random stem cell in the brain of each. The idea was to create a population of larvae in which each of the 100 or so neural stem cells was labeled at least once. When the larvae grew to adults, the researchers examined the flies’ brains using confocal microscopy. With this technique, the part of a fly’s brain that derived from a single, labeled stem cell “lights up.” The scientists photographed each brain and digitally colorized its lit-up area. By combining thousands of such photos, they created a three-dimensional, color-coded map that shows which part of the Drosophila brain comes from each of its ~100 neural stem cells. In other words, each colored region shows which neurons are the progeny or “clones” of a single stem cell. This work established a hierarchical structure as well as nomenclature for the neurons in the Drosophila brain. Further research will relate functions to structures of the brain.
Related to images 5838 and 5868.
Related to images 5838 and 5868.
Yong Wan from Charles Hansen’s lab, University of Utah. Data preparation and visualization by Masayoshi Ito in the lab of Kei Ito, University of Tokyo.
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6850: Himastatin and bacteria
6850: Himastatin and bacteria
A model of the molecule himastatin overlaid on an image of Bacillus subtilis bacteria. Scientists first isolated himastatin from the bacterium Streptomyces himastatinicus, and the molecule shows antibiotic activity. The researchers who created this image developed a new, more concise way to synthesize himastatin so it can be studied more easily. They also tested the effects of himastatin and derivatives of the molecule on B. subtilis.
More information about the research that produced this image can be found in the Science paper “Total synthesis of himastatin” by D’Angelo et al.
Related to image 6848 and video 6851.
More information about the research that produced this image can be found in the Science paper “Total synthesis of himastatin” by D’Angelo et al.
Related to image 6848 and video 6851.
Mohammad Movassaghi, Massachusetts Institute of Technology.
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3650: How a microtubule builds and deconstructs
3650: How a microtubule builds and deconstructs
A microtubule, part of the cell's skeleton, builds and deconstructs.
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3392: NCMIR Kidney Glomeruli
3392: NCMIR Kidney Glomeruli
Stained glomeruli in the kidney. The kidney is an essential organ responsible for disposing wastes from the body and for maintaining healthy ion levels in the blood. It works like a purifier by pulling break-down products of metabolism, such as urea and ammonium, from the bloodstream for excretion in urine. The glomerulus is a structure that helps filter the waste compounds from the blood. It consists of a network of capillaries enclosed within a Bowman's capsule of a nephron, which is the structure in which ions exit or re-enter the blood in the kidney.
Tom Deerinck, National Center for Microscopy and Imaging Research (NCMIR)
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2779: Mature, flowering Arabidopsis
2779: Mature, flowering Arabidopsis
This is an adult flowering Arabidopsis thaliana plant with the inbred designation L-er. Arabidopsis is the most widely used model organism for researchers who study plant genetics.
Jeff Dangl, University of North Carolina, Chapel Hill
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1015: Lily mitosis 05
1015: Lily mitosis 05
A light microscope image of a cell from the endosperm of an African globe lily (Scadoxus katherinae). This is one frame of a time-lapse sequence that shows cell division in action. The lily is considered a good organism for studying cell division because its chromosomes are much thicker and easier to see than human ones. Staining shows microtubules in red and chromosomes in blue. Here, condensed chromosomes are clearly visible.
Related to images 1010, 1011, 1012, 1013, 1014, 1016, 1017, 1018, 1019, and 1021.
Related to images 1010, 1011, 1012, 1013, 1014, 1016, 1017, 1018, 1019, and 1021.
Andrew S. Bajer, University of Oregon, Eugene
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2354: Section of an electron density map
2354: Section of an electron density map
Electron density maps such as this one are generated from the diffraction patterns of X-rays passing through protein crystals. These maps are then used to generate a model of the protein's structure by fitting the protein's amino acid sequence (yellow) into the observed electron density (blue).
The Southeast Collaboratory for Structural Genomics
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6593: Cell-like compartments from frog eggs 6
6593: Cell-like compartments from frog eggs 6
Cell-like compartments that spontaneously emerged from scrambled frog eggs, with nuclei (blue) from frog sperm. Endoplasmic reticulum (red) and microtubules (green) are also visible. Image created using confocal microscopy.
For more photos of cell-like compartments from frog eggs view: 6584, 6585, 6586, 6591, 6592.
For videos of cell-like compartments from frog eggs view: 6587, 6588, 6589, and 6590.
Xianrui Cheng, Stanford University School of Medicine.
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