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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.

5751: Genetically identical mycobacteria respond differently to antibiotic 1
5751: Genetically identical mycobacteria respond differently to antibiotic 1
Antibiotic resistance in microbes is a serious health concern. So researchers have turned their attention to how bacteria undo the action of some antibiotics. Here, scientists set out to find the conditions that help individual bacterial cells survive in the presence of the antibiotic rifampicin. The research team used Mycobacterium smegmatis, a more harmless relative of Mycobacterium tuberculosis, which infects the lung and other organs and causes serious disease.
In this image, genetically identical mycobacteria are growing in a miniature growth chamber called a microfluidic chamber. Using live imaging, the researchers found that individual mycobacteria will respond differently to the antibiotic, depending on the growth stage and other timing factors. The researchers used genetic tagging with green fluorescent protein to distinguish cells that can resist rifampicin and those that cannot. With this gene tag, cells tolerant of the antibiotic light up in green and those that are susceptible in violet, enabling the team to monitor the cells' responses in real time.
To learn more about how the researchers studied antibiotic resistance in mycobacteria, see this news release from Tufts University. Related to video 5752.
In this image, genetically identical mycobacteria are growing in a miniature growth chamber called a microfluidic chamber. Using live imaging, the researchers found that individual mycobacteria will respond differently to the antibiotic, depending on the growth stage and other timing factors. The researchers used genetic tagging with green fluorescent protein to distinguish cells that can resist rifampicin and those that cannot. With this gene tag, cells tolerant of the antibiotic light up in green and those that are susceptible in violet, enabling the team to monitor the cells' responses in real time.
To learn more about how the researchers studied antibiotic resistance in mycobacteria, see this news release from Tufts University. Related to video 5752.
Bree Aldridge, Tufts University
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2361: Chromium X-ray source
2361: Chromium X-ray source
In the determination of protein structures by X-ray crystallography, this unique soft (l = 2.29Å) X-ray source is used to collect anomalous scattering data from protein crystals containing light atoms such as sulfur, calcium, zinc and phosphorous. These data can be used to image the protein.
The Southeast Collaboratory for Structural Genomics
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1286: Animal cell membrane
1286: Animal cell membrane
The membrane that surrounds a cell is made up of proteins and lipids. Depending on the membrane's location and role in the body, lipids can make up anywhere from 20 to 80 percent of the membrane, with the remainder being proteins. Cholesterol (green), which is not found in plant cells, is a type of lipid that helps stiffen the membrane.
Judith Stoffer
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3574: Cytonemes in developing fruit fly cells
3574: Cytonemes in developing fruit fly cells
Scientists have long known that multicellular organisms use biological molecules produced by one cell and sensed by another to transmit messages that, for instance, guide proper development of organs and tissues. But it's been a puzzle as to how molecules dumped out into the fluid-filled spaces between cells can precisely home in on their targets. Using living tissue from fruit flies, a team led by Thomas Kornberg of the University of California, San Francisco, has shown that typical cells in animals can talk to each other via long, thin cell extensions called cytonemes (Latin for "cell threads") that may span the length of 50 or 100 cells. The point of contact between a cytoneme and its target cell acts as a communications bridge between the two cells.
Sougata Roy, University of California, San Francisco
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3479: Electrode probe on mouse Huntington's muscle cell
3479: Electrode probe on mouse Huntington's muscle cell
Using an electrode, researchers apply an electrical pulse onto a piece of muscle tissue affected by Huntington's disease.
Grigor Varuzhanyan and Andrew A. Voss, California State Polytechnic University
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3628: Skin cancer cells (squamous cell carcinoma)
3628: Skin cancer cells (squamous cell carcinoma)
This image shows the uncontrolled growth of cells in squamous cell carcinoma, the second most common form of skin cancer. If caught early, squamous cell carcinoma is usually not life-threatening.
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.
Markus Schober and Elaine Fuchs, The Rockefeller University
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5857: 3D reconstruction of a tubular matrix in peripheral endoplasmic reticulum
5857: 3D reconstruction of a tubular matrix in peripheral endoplasmic reticulum
Detailed three-dimensional reconstruction of a tubular matrix in a thin section of the peripheral endoplasmic reticulum between the plasma membranes of the cell. The endoplasmic reticulum (ER) is a continuous membrane that extends like a net from the envelope of the nucleus outward to the cell membrane. The ER plays several roles within the cell, such as in protein and lipid synthesis and transport of materials between organelles. Shown here is a three-dimensional representation of the peripheral ER microtubules. Related to images 5855 and 5856
Jennifer Lippincott-Schwartz, Howard Hughes Medical Institute Janelia Research Campus, Virginia
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2392: Sheep hemoglobin crystal
2392: Sheep hemoglobin crystal
A crystal of sheep hemoglobin protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.
Alex McPherson, University of California, Irvine
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2373: Oligoendopeptidase F from B. stearothermophilus
2373: Oligoendopeptidase F from B. stearothermophilus
Crystal structure of oligoendopeptidase F, a protein slicing enzyme from Bacillus stearothermophilus, a bacterium that can cause food products to spoil. The crystal was formed using a microfluidic capillary, a device that enables scientists to independently control the parameters for protein crystal nucleation and growth. Featured as one of the July 2007 Protein Structure Initiative Structures of the Month.
Accelerated Technologies Center for Gene to 3D Structure/Midwest Center for Structural Genomics
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2702: Thermotoga maritima and its metabolic network
2702: Thermotoga maritima and its metabolic network
A combination of protein structures determined experimentally and computationally shows us the complete metabolic network of a heat-loving bacterium.
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2304: Bacteria working to eat
2304: Bacteria working to eat
Gram-negative bacteria perform molecular acrobatics just to eat. Because they're encased by two membranes, they must haul nutrients across both. To test one theory of how the bacteria manage this feat, researchers used computer simulations of two proteins involved in importing vitamin B12. Here, the protein (red) anchored in the inner membrane of bacteria tugs on a much larger protein (green and blue) in the outer membrane. Part of the larger protein unwinds, creating a pore through which the vitamin can pass.
Emad Tajkhorshid, University of Illinois at Urbana-Champaign
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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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6613: Circadian rhythms and the SCN
6613: Circadian rhythms and the SCN
Circadian rhythms are physical, mental, and behavioral changes that follow a 24-hour cycle. Circadian rhythms are influenced by light and regulated by the brain’s suprachiasmatic nucleus (SCN), sometimes referred to as a master clock. Learn more in NIGMS’ circadian rhythms fact sheet. See 6614 for the Spanish version of this infographic.
NIGMS
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6607: Cryo-ET cell cross-section visualizing insulin vesicles
6607: Cryo-ET cell cross-section visualizing insulin vesicles
On the left, a cross-section slice of a rat pancreas cell captured using cryo-electron tomography (cryo-ET). On the right, a color-coded, 3D version of the image highlighting cell structures. Visible features include insulin vesicles (purple rings), insulin crystals (gray circles), microtubules (green rods), ribosomes (small yellow circles). The black line at the bottom right of the left image represents 200 nm. Related to image 6608.
Xianjun Zhang, University of Southern California.
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2384: Scientists display X-ray diffraction pattern obtained with split X-ray beamline
2384: Scientists display X-ray diffraction pattern obtained with split X-ray beamline
Scientists from Argonne National Laboratory's Advanced Photon Source (APS) display the first X-ray diffraction pattern obtained from a protein crystal using a split X-ray beam, the first of its kind at APS. The scientists shown are (from left to right): Oleg Makarov, Ruslan Sanishvili, Robert Fischetti (project manager), Sergey Stepanov, and Ward Smith.
GM/CA Collaborative Access Team
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5866: Structure of a key antigen protein involved with Hepatitis C Virus infection
5866: Structure of a key antigen protein involved with Hepatitis C Virus infection
A three-dimensional representation of the structure of E2, a key antigen protein involved with hepatitis C virus infection.
Mansun Law Associate Professor Department of Immunolgy and Microbial Science The Scripps Research Institute
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3275: Human embryonic stem cells on feeder cells
3275: Human embryonic stem cells on feeder cells
The nuclei stained green highlight human embryonic stem cells grown under controlled conditions in a laboratory. Blue represents the DNA of surrounding, supportive feeder cells. Image and caption information courtesy of the California Institute for Regenerative Medicine. See related image 3724.
Julie Baker lab, Stanford University School of Medicine, via CIRM
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2539: Chromosome inside nucleus
2539: Chromosome inside nucleus
The long, stringy DNA that makes up genes is spooled within chromosomes inside the nucleus of a cell. (Note that a gene would actually be a much longer stretch of DNA than what is shown here.) See image 2540 for a labeled version of this illustration. Featured in The New Genetics.
Crabtree + Company
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2343: Protein rv2844 from M. tuberculosis
2343: Protein rv2844 from M. tuberculosis
This crystal structure shows a conserved hypothetical protein from Mycobacterium tuberculosis. Only 12 other proteins share its sequence homology, and none has a known function. This structure indicates the protein may play a role in metabolic pathways. Featured as one of the August 2007 Protein Structure Initiative Structures of the Month.
Integrated Center for Structure and Function Innovation
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2440: Hydra 04
2440: Hydra 04
Hydra magnipapillata is an invertebrate animal used as a model organism to study developmental questions, for example the formation of the body axis.
Hiroshi Shimizu, National Institute of Genetics in Mishima, Japan
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3614: Birth of a yeast cell
3614: Birth of a yeast cell
Yeast make bread, beer, and wine. And like us, yeast can reproduce sexually. A mother and father cell fuse and create one large cell that contains four offspring. When environmental conditions are favorable, the offspring are released, as shown here. Yeast are also a popular study subject for scientists. Research on yeast has yielded vast knowledge about basic cellular and molecular biology as well as about myriad human diseases, including colon cancer and various metabolic disorders.
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.
Juergen Berger, Max Planck Institute for Developmental Biology, and Maria Langegger, Friedrich Miescher Laboratory of the Max Planck Society, Germany
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3419: X-ray co-crystal structure of Src kinase bound to a DNA-templated macrocycle inhibitor 7
3419: X-ray co-crystal structure of Src kinase bound to a DNA-templated macrocycle inhibitor 7
X-ray co-crystal structure of Src kinase bound to a DNA-templated macrocycle inhibitor. Related to images 3413, 3414, 3415, 3416, 3417, and 3418.
Markus A. Seeliger, Stony Brook University Medical School and David R. Liu, Harvard University
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1021: Lily mitosis 08
1021: Lily mitosis 08
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 and lined up.
Related to images 1010, 1011, 1012, 1013, 1014, 1015, 1016, 1017, 1018, and 1019.
Related to images 1010, 1011, 1012, 1013, 1014, 1015, 1016, 1017, 1018, and 1019.
Andrew S. Bajer, University of Oregon, Eugene
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3295: Cluster analysis of mysterious protein
3295: Cluster analysis of mysterious protein
Researchers use cluster analysis to study protein shape and function. Each green circle represents one potential shape of the protein mitoNEET. The longer the blue line between two circles, the greater the differences between the shapes. Most shapes are similar; they fall into three clusters that are represented by the three images of the protein. From a Rice University news release. Graduate student Elizabeth Baxter and Patricia Jennings, professor of chemistry and biochemistry at UCSD, collaborated with José Onuchic, a physicist at Rice University, on this work.
Patricia Jennings and Elizabeth Baxter, University of California, San Diego
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5795: Mouse cerebellum
5795: Mouse cerebellum
The cerebellum is the brain's locomotion control center. Found at the base of your brain, the cerebellum is a single layer of tissue with deep folds like an accordion. People with damage to this region of the brain often have difficulty with balance, coordination and fine motor skills.
This image of a mouse cerebellum is part of a collection of such images in different colors and at different levels of magnification from the National Center for Microscopy and Imaging Research (NCMIR). Related to image 5800.
This image of a mouse cerebellum is part of a collection of such images in different colors and at different levels of magnification from the National Center for Microscopy and Imaging Research (NCMIR). Related to image 5800.
National Center for Microscopy and Imaging Research (NCMIR)
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6389: Red and white blood cells in the lung

3434: Flu virus proteins during self-replication
3434: Flu virus proteins during self-replication
Influenza (flu) virus proteins in the act of self-replication. Viral nucleoprotein (blue) encapsidates [encapsulates] the RNA genome (green). The influenza virus polymerase (orange) reads and copies the RNA genome. In the background is an image of influenza virus ribonucleoprotein complexes observed using cryo-electron microscopy. This image is from a November 2012 News Release.
Scripps Research Institute in La Jolla, CA
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2782: Disease-susceptible Arabidopsis leaf
2782: Disease-susceptible Arabidopsis leaf
This is a magnified view of an Arabidopsis thaliana leaf after several days of infection with the pathogen Hyaloperonospora arabidopsidis. The pathogen's blue hyphae grow throughout the leaf. On the leaf's edges, stalk-like structures called sporangiophores are beginning to mature and will release the pathogen's spores. Inside the leaf, the large, deep blue spots are structures called oopsorangia, also full of spores. Compare this response to that shown in Image 2781. Jeff Dangl has been funded by NIGMS to study the interactions between pathogens and hosts that allow or suppress infection.
Jeff Dangl, University of North Carolina, Chapel Hill
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2763: Fused, dicentric chromosomes
2763: Fused, dicentric chromosomes
This fused chromosome has two functional centromeres, shown as two sets of red and green dots. Centromeres are DNA/protein complexes that are key to splitting the chromosomes evenly during cell division. When dicentric chromosomes like this one are formed in a person, fertility problems or other difficulties may arise. Normal chromosomes carrying a single centromere (one set of red and green dots) are also visible in this image.
Beth A. Sullivan, Duke University
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3527: Bacteria in the mouse colon
3527: Bacteria in the mouse colon
Image of the colon of a mouse mono-colonized with Bacteroides fragilis (red) residing within the crypt channel. The red staining is due to an antibody to B. fragilis, the green staining is a general dye for the mouse cells (phalloidin, which stains F-actin) and the light blue glow is from a dye for visualizing the mouse cell nuclei (DAPI, which stains DNA). Bacteria from the human microbiome have evolved specific molecules to physically associate with host tissue, conferring resilience and stability during life-long colonization of the gut. Image is featured in October 2015 Biomedical Beat blog post Cool Images: A Halloween-Inspired Cell Collection.
Sarkis K. Mazmanian, California Institute of Technology
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2795: Anti-tumor drug ecteinascidin 743 (ET-743), structure without hydrogens 02
2795: Anti-tumor drug ecteinascidin 743 (ET-743), structure without hydrogens 02
Ecteinascidin 743 (ET-743, brand name Yondelis), was discovered and isolated from a sea squirt, Ecteinascidia turbinata, by NIGMS grantee Kenneth Rinehart at the University of Illinois. It was synthesized by NIGMS grantees E.J. Corey and later by Samuel Danishefsky. Multiple versions of this structure are available as entries 2790-2797.
Timothy Jamison, Massachusetts Institute of Technology
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6755: Honeybee brain
6755: Honeybee brain
Insect brains, like the honeybee brain shown here, are very different in shape from human brains. Despite that, bee and human brains have a lot in common, including many of the genes and neurochemicals they rely on in order to function. The bright-green spots in this image indicate the presence of tyrosine hydroxylase, an enzyme that allows the brain to produce dopamine. Dopamine is involved in many important functions, such as the ability to experience pleasure. This image was captured using confocal microscopy.
Gene Robinson, University of Illinois at Urbana-Champaign.
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3678: STORM image of axonal cytoskeleton
3678: STORM image of axonal cytoskeleton
This image shows the long, branched structures (axons) of nerve cells. Running horizontally across the middle of the photo is an axon wrapped in rings made of actin protein (green), which plays important roles in nerve cells. The image was captured with a powerful microscopy technique that allows scientists to see single molecules in living cells in real time. The technique is called stochastic optical reconstruction microscopy (STORM). It is based on technology so revolutionary that its developers earned the 2014 Nobel Prize in Chemistry. More information about this image can be found in: K. Xu, G. Zhong, X. Zhuang. Actin, spectrin and associated proteins form a periodic cytoskeleton structure in axons. Science 339, 452-456 (2013).
Xiaowei Zhuang Laboratory, Howard Hughes Medical Institute, Harvard University
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2395: Fungal lipase (1)
2395: Fungal lipase (1)
Crystals of fungal lipase protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.
Alex McPherson, University of California, Irvine
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1316: Mitosis - interphase
1316: Mitosis - interphase
A cell in interphase, at the start of mitosis: Chromosomes duplicate, and the copies remain attached to each other. Mitosis is responsible for growth and development, as well as for replacing injured or worn out cells throughout the body. For simplicity, mitosis is illustrated here with only six chromosomes.
Judith Stoffer
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2351: tRNA splicing enzyme endonuclease in humans
2351: tRNA splicing enzyme endonuclease in humans
An NMR solution structure model of the transfer RNA splicing enzyme endonuclease in humans (subunit Sen15). This represents the first structure of a eukaryotic tRNA splicing endonuclease subunit.
Center for Eukaryotic Structural Genomics, PSI
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3279: Induced pluripotent stem cells from skin 02
3279: Induced pluripotent stem cells from skin 02
These induced pluripotent stem cells (iPS cells) were derived from a woman's skin. Blue show nuclei. Green show a protein found in iPS cells but not in skin cells (NANOG). The red dots show the inactivated X chromosome in each cell. These cells can develop into a variety of cell types. Image and caption information courtesy of the California Institute for Regenerative Medicine. Related to image 3278.
Kathrin Plath lab, University of California, Los Angeles, via CIRM
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3792: Nucleolus subcompartments spontaneously self-assemble 3
3792: Nucleolus subcompartments spontaneously self-assemble 3
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 3793.
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 3793.
Nilesh Vaidya, Princeton University
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6848: Himastatin
6848: Himastatin
A model of the molecule himastatin, which was first isolated from the bacterium Streptomyces himastatinicus. Himastatin 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.
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 6850 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 6850 and video 6851.
Mohammad Movassaghi, Massachusetts Institute of Technology.
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1285: Lipid raft
1285: Lipid raft
Researchers have learned much of what they know about membranes by constructing artificial membranes in the laboratory. In artificial membranes, different lipids separate from each other based on their physical properties, forming small islands called lipid rafts.
Judith Stoffer
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6811: Fruit fly egg chamber
6811: Fruit fly egg chamber
A fruit fly (Drosophila melanogaster) egg chamber with microtubules shown in green and actin filaments shown in red. Egg chambers are multicellular structures in fruit flies ovaries that each give rise to a single egg. Microtubules and actin filaments give the chambers structure and shape. This image was captured using a confocal microscope.
More information on the research that produced this image can be found in the Current Biology paper "Gatekeeper function for Short stop at the ring canals of the Drosophila ovary" by Lu et al.
More information on the research that produced this image can be found in the Current Biology paper "Gatekeeper function for Short stop at the ring canals of the Drosophila ovary" by Lu et al.
Vladimir I. Gelfand, Feinberg School of Medicine, Northwestern University.
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1251: Crab larva eye
1251: Crab larva eye
Colorized scanning electron micrographs progressively zoom in on the eye of a crab larva. In the higher-resolution frames, bacteria are visible on the eye.
Tina Weatherby Carvalho, University of Hawaii at Manoa
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2400: Pig trypsin (1)
2400: Pig trypsin (1)
A crystal of porcine trypsin protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.
Alex McPherson, University of California, Irvine
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3725: Fluorescent microscopy of kidney tissue--close-up
3725: Fluorescent microscopy of kidney tissue--close-up
This photograph of kidney tissue, taken using fluorescent light microscopy, shows a close-up view of part of image 3723. Kidneys filter the blood, removing waste and excessive fluid, which is excreted in urine. The filtration system is made up of components that include glomeruli (for example, the round structure taking up much of the image's center is a glomerulus) and tubules (seen in cross-section here with their inner lining stained green). Related to image 3675 .
Tom Deerinck , National Center for Microscopy and Imaging Research
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7014: Flagellated bacterial cells
7014: Flagellated bacterial cells
Vibrio fischeri (2 mm in length) is the exclusive symbiotic partner of the Hawaiian bobtail squid, Euprymna scolopes. After this bacterium uses its flagella to swim from the seawater into the light organ of a newly hatched juvenile, it colonizes the host and loses the appendages. This image was taken using a scanning electron microscope.
Margaret J. McFall-Ngai, Carnegie Institution for Science/California Institute of Technology, and Edward G. Ruby, California Institute of Technology.
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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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1241: Borrelia burgdorferi
1241: Borrelia burgdorferi
Borrelia burgdorferi is a spirochete, a class of long, slender bacteria that typically take on a coiled shape. Infection with this bacterium causes Lyme disease.
Tina Weatherby Carvalho, University of Hawaii at Manoa
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5875: Bacteriophage P22 capsid, detail
5875: Bacteriophage P22 capsid, detail
Detail of a subunit of the capsid, or outer cover, of bacteriophage P22, a virus that infects the Salmonella bacteria. Cryo-electron microscopy (cryo-EM) was used to capture details of the capsid proteins, each shown here in a separate color. Thousands of cryo-EM scans capture the structure and shape of all the individual proteins in the capsid and their position relative to other proteins. A computer model combines these scans into the image shown here. Related to image 5874.
Dr. Wah Chiu, Baylor College of Medicine
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3254: Pulsating response to stress in bacteria - video
3254: Pulsating response to stress in bacteria - video
By attaching fluorescent proteins to the genetic circuit responsible for B. subtilis's stress response, researchers can observe the cells' pulses as green flashes. This video shows flashing cells as they multiply over the course of more than 12 hours. In response to a stressful environment like one lacking food, B. subtilis activates a large set of genes that help it respond to the hardship. Instead of leaving those genes on as previously thought, researchers discovered that the bacteria flip the genes on and off, increasing the frequency of these pulses with increasing stress. See entry 3253 for a related still image.
Michael Elowitz, Caltech University
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2509: From DNA to Protein
2509: From DNA to Protein
Nucleotides in DNA are copied into RNA, where they are read three at a time to encode the amino acids in a protein. Many parts of a protein fold as the amino acids are strung together.
See image 2510 for a labeled version of this illustration.
Featured in The Structures of Life.
See image 2510 for a labeled version of this illustration.
Featured in The Structures of Life.
Crabtree + Company
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