Switch to List View
Image and Video Gallery
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.
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
View Media
3493: Repairing DNA
3493: Repairing DNA
Like a watch wrapped around a wrist, a special enzyme encircles the double helix to repair a broken strand of DNA. Without molecules that can mend such breaks, cells can malfunction, die, or become cancerous. Related to image 2330.
Tom Ellenberger, Washington University School of Medicine
View Media
1058: Lily mitosis 01
1058: Lily mitosis 01
A light microscope image shows the chromosomes, stained dark blue, in a dividing cell 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.
Andrew S. Bajer, University of Oregon, Eugene
View Media
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
View Media
5811: NCMIR Tongue 2
5811: NCMIR Tongue 2
Microscopy image of a tongue. One in a series of two, see image 5810
National Center for Microscopy and Imaging Research (NCMIR)
View Media
2338: Tex protein
2338: Tex protein
Model of a member from the Tex protein family, which is implicated in transcriptional regulation and highly conserved in eukaryotes and prokaryotes. The structure shows significant homology to a human transcription elongation factor that may regulate multiple steps in mRNA synthesis.
New York Structural GenomiX Research Consortium, PSI
View Media
3550: Protein clumping in zinc-deficient yeast cells
3550: Protein clumping in zinc-deficient yeast cells
The green spots in this image are clumps of protein inside yeast cells that are deficient in both zinc and a protein called Tsa1 that prevents clumping. Protein clumping plays a role in many diseases, including Parkinson's and Alzheimer's, where proteins clump together in the brain. Zinc deficiency within a cell can cause proteins to mis-fold and eventually clump together. Normally, in yeast, Tsa1 codes for so-called "chaperone proteins" which help proteins in stressed cells, such as those with a zinc deficiency, fold correctly. The research behind this image was published in 2013 in the Journal of Biological Chemistry.
Colin MacDiarmid and David Eide, University of Wisconsin--Madison
View Media
7003: Catalase diversity
7003: Catalase diversity
Catalases are some of the most efficient enzymes found in cells. Each catalase molecule can decompose millions of hydrogen peroxide molecules every second—working as an antioxidant to protect cells from the dangerous form of reactive oxygen. Different cells build different types of catalases. The human catalase that protects our red blood cells, shown on the left from PDB entry 1QQW, is composed of four identical subunits and uses a heme/iron group to perform the reaction. Many bacteria scavenge hydrogen peroxide with a larger catalase, shown in the center from PDB entry 1IPH, that uses a similar arrangement of iron and heme. Other bacteria protect themselves with an entirely different catalase that uses manganese ions instead of heme, as shown at the right from PDB entry 1JKU.
Amy Wu and Christine Zardecki, RCSB Protein Data Bank.
View Media
3791: Nucleolus subcompartments spontaneously self-assemble 2
3791: Nucleolus subcompartments spontaneously self-assemble 2
The nucleolus is 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 video of nucleoli in the eggs of a commonly used lab animal, the frog Xenopus laevis, shows how each of the compartments (the granular component is shown in red, the fibrillarin in yellow-green, and the fibrillar center in blue) 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, image 3792 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 video of nucleoli in the eggs of a commonly used lab animal, the frog Xenopus laevis, shows how each of the compartments (the granular component is shown in red, the fibrillarin in yellow-green, and the fibrillar center in blue) 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, image 3792 and image 3793.
Nilesh Vaidya, Princeton University
View Media
3624: Fibroblasts with nuclei in blue, energy factories in green and the actin cytoskeleton in red
3624: Fibroblasts with nuclei in blue, energy factories in green and the actin cytoskeleton in red
The cells shown here are fibroblasts, one of the most common cells in mammalian connective tissue. These particular cells were taken from a mouse embryo. Scientists used them to test the power of a new microscopy technique that offers vivid views of the inside of a cell. The DNA within the nucleus (blue), mitochondria (green), and actin filaments in the cellular skeleton (red) are clearly visible.
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.
Dylan Burnette, NICHD
View Media
6570: Stress Response in Cells
6570: Stress Response in Cells
Two highly stressed osteosarcoma cells are shown with a set of green droplet-like structures followed by a second set of magenta droplets. These droplets are composed of fluorescently labeled stress-response proteins, either G3BP or UBQLN2 (Ubiquilin-2). Each protein is undergoing a fascinating process, called phase separation, in which a non-membrane bound compartment of the cytoplasm emerges with a distinct environment from the surrounding cytoplasm. Subsequently, the proteins fuse with like proteins to form larger droplets, in much the same way that raindrops merge on a car’s windshield.
Julia F. Riley and Carlos A. Castañeda, Syracuse University
View Media
2549: Central dogma, illustrated (with labels and numbers for stages)
2549: Central dogma, illustrated (with labels and numbers for stages)
DNA encodes RNA, which encodes protein. DNA is transcribed to make messenger RNA (mRNA). The mRNA sequence (dark red strand) is complementary to the DNA sequence (blue strand). On ribosomes, transfer RNA (tRNA) reads three nucleotides at a time in mRNA to bring together the amino acids that link up to make a protein. See image 2548 for a version of this illustration that isn't numbered and 2547 for a an entirely unlabeled version. Featured in The New Genetics.
Crabtree + Company
View Media
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
View Media
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
View Media
6352: CRISPR surveillance complex
6352: CRISPR surveillance complex
This image shows how the CRISPR surveillance complex is disabled by two copies of anti-CRISPR protein AcrF1 (red) and one AcrF2 (light green). These anti-CRISPRs block access to the CRISPR RNA (green tube) preventing the surveillance complex from scanning and targeting invading viral DNA for destruction.
NRAMM National Resource for Automated Molecular Microscopy http://nramm.nysbc.org/nramm-images/ Source: Bridget Carragher
View Media
5780: Ribosome illustration from PDB
5780: Ribosome illustration from PDB
Ribosomes are complex machines made up of more than 50 proteins and three or four strands of genetic material called ribosomal RNA (rRNA). The busy cellular machines make proteins, which are critical to almost every structure and function in the cell. To do so, they read protein-building instructions, which come as strands of messenger RNA. Ribosomes are found in all forms of cellular life—people, plants, animals, even bacteria. This illustration of a bacterial ribosome was produced using detailed information about the position of every atom in the complex. Several antibiotic medicines work by disrupting bacterial ribosomes but leaving human ribosomes alone. Scientists are carefully comparing human and bacterial ribosomes to spot differences between the two. Structures that are present only in the bacterial version could serve as targets for new antibiotic medications.
From PDB’s Molecule of the Month collection (direct link: http://pdb101.rcsb.org/motm/121) Molecule of the Month illustrations are available under a CC-BY-4.0 license. Attribution should be given to David S. Goodsell and the RCSB PDB.
View Media
2604: Induced stem cells from adult skin 02
2604: Induced stem cells from adult skin 02
These cells are induced stem cells made from human adult skin cells that were genetically reprogrammed to mimic embryonic stem cells. The induced stem cells were made potentially safer by removing the introduced genes and the viral vector used to ferry genes into the cells, a loop of DNA called a plasmid. The work was accomplished by geneticist Junying Yu in the laboratory of James Thomson, a University of Wisconsin-Madison School of Medicine and Public Health professor and the director of regenerative biology for the Morgridge Institute for Research.
James Thomson, University of Wisconsin-Madison
View Media
2841: Circadian rhythm
2841: Circadian rhythm
The human body keeps time with a master clock called the suprachiasmatic nucleus or SCN. Situated inside the brain, it's a tiny sliver of tissue about the size of a grain of rice, located behind the eyes. It sits quite close to the optic nerve, which controls vision, and this means that the SCN "clock" can keep track of day and night. The SCN helps control sleep by coordinating the actions of billions of miniature "clocks" throughout the body. These aren't actually clocks, but rather are ensembles of genes inside clusters of cells that switch on and off in a regular, 24-hour cycle in our physiological day.
Crabtree + Company
View Media
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
View Media
2483: Trp_RS - tryptophanyl tRNA-synthetase family of enzymes
2483: Trp_RS - tryptophanyl tRNA-synthetase family of enzymes
This image represents the structure of TrpRS, a novel member of the tryptophanyl tRNA-synthetase family of enzymes. By helping to link the amino acid tryptophan to a tRNA molecule, TrpRS primes the amino acid for use in protein synthesis. A cluster of iron and sulfur atoms (orange and red spheres) was unexpectedly found in the anti-codon domain, a key part of the molecule, and appears to be critical for the function of the enzyme. TrpRS was discovered in Thermotoga maritima, a rod-shaped bacterium that flourishes in high temperatures.
View Media
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
View Media
2744: Dynamin structure
2744: Dynamin structure
When a molecule arrives at a cell's outer membrane, the membrane creates a pouch around the molecule that protrudes inward. Directed by a protein called dynamin, the pouch then gets pinched off to form a vesicle that carries the molecule to the right place inside the cell. To better understand how dynamin performs its vital pouch-pinching role, researchers determined its structure. Based on the structure, they proposed that a dynamin "collar" at the pouch's base twists ever tighter until the vesicle pops free. Because cells absorb many drugs through vesicles, the discovery could lead to new drug delivery methods.
Josh Chappie, National Institute of Diabetes and Digestive and Kidney Diseases, NIH
View Media
3332: Polarized cells- 01
3332: Polarized cells- 01
Cells move forward with lamellipodia and filopodia supported by networks and bundles of actin filaments. Proper, controlled cell movement is a complex process. Recent research has shown that an actin-polymerizing factor called the Arp2/3 complex is the key component of the actin polymerization engine that drives amoeboid cell motility. ARPC3, a component of the Arp2/3 complex, plays a critical role in actin nucleation. In this photo, the ARPC3+/+ fibroblast cells were fixed and stained with Alexa 546 phalloidin for F-actin (red) and DAPI to visualize the nucleus (blue). ARPC3+/+ fibroblast cells with lamellipodia leading edge. Related to images 3328, 3329, 3330, 3331, and 3333.
Rong Li and Praveen Suraneni, Stowers Institute for Medical Research
View Media
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.
View Media
1282: Lysosomes
1282: Lysosomes
Lysosomes have powerful enzymes and acids to digest and recycle cell materials.
Judith Stoffer
View Media
1337: Bicycling cell
1337: Bicycling cell
A humorous treatment of the concept of a cycling cell.
Judith Stoffer
View Media
6521: Yeast art depicting the New York City skyline
6521: Yeast art depicting the New York City skyline
This skyline of New York City was created by “printing” nanodroplets containing yeast (Saccharomyces cerevisiae) onto a large plate. Each dot is a separate yeast colony. As the colonies grew, a picture emerged, creating art. To make the different colors shown here, yeast strains were genetically engineered to produce pigments naturally made by bacteria, fungi, and sea creatures such as coral and sea anemones. Using genes from other organisms to make biological compounds paves the way toward harnessing yeast in the production of other useful molecules, from food to fuels and drugs.
Michael Shen, Ph.D., Jasmine Temple, Leslie Mitchell, Ph.D., and Jef Boeke, Ph.D., New York University School of Medicine; and Nick Phillips, James Chuang, Ph.D., and Jiarui Wang, Johns Hopkins University.
View Media
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
View Media
6928: Axolotls showing nervous system components
6928: Axolotls showing nervous system components
Axolotls—a type of salamander—that have been genetically modified so that various parts of their nervous systems glow purple and green. Researchers often study axolotls for their extensive regenerative abilities. They can regrow tails, limbs, spinal cords, brains, and more. The researcher who took this image focuses on the role of the peripheral nervous system during limb regeneration.
This image was captured using a stereo microscope.
Related to images 6927 and 6932.
This image was captured using a stereo microscope.
Related to images 6927 and 6932.
Prayag Murawala, MDI Biological Laboratory and Hannover Medical School.
View Media
6538: Pathways: The Fascinating Cells of Research Organisms
6538: Pathways: The Fascinating Cells of Research Organisms
Learn how research organisms, such as fruit flies and mice, can help us understand and treat human diseases. Discover more resources from NIGMS’ Pathways collaboration with Scholastic. View the video on YouTube for closed captioning.
National Institute of General Medical Sciences
View Media
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
View Media
2379: Secreted protein from Mycobacteria
2379: Secreted protein from Mycobacteria
Model of a major secreted protein of unknown function, which is only found in mycobacteria, the class of bacteria that causes tuberculosis. Based on structural similarity, this protein may be involved in host-bacterial interactions.
Mycobacterium Tuberculosis Center, PSI
View Media
2545: Meiosis illustration
2545: Meiosis illustration
Meiosis is the process whereby a cell reduces its chromosomes from diploid to haploid in creating eggs or sperm. See image 2546 for a labeled version of this illustration. Featured in The New Genetics.
Crabtree + Company
View Media
2309: Cellular polarity
2309: Cellular polarity
As an egg cell develops, a process called polarization controls what parts ultimately become the embryo's head and tail. This picture shows an egg of the fruit fly Drosophila. Red and green mark two types of signaling proteins involved in polarization. Disrupting these signals can scramble the body plan of the embryo, leading to severe developmental disorders.
Wu-Min Deng, Florida State University
View Media
3286: Retinal pigment epithelium derived from human ES cells
3286: Retinal pigment epithelium derived from human ES cells
This color-enhanced image is a scanning electron microscope image of retinal pigment epithelial (RPE) cells derived from human embryonic stem cells. The cells are remarkably similar to normal RPE cells, growing in a hexagonal shape in a single, well-defined layer. This kind of retinal cell is responsible for macular degeneration, the most common cause of blindness. Image and caption information courtesy of the California Institute for Regenerative Medicine. Related to image 3287.
David Hinton lab, University of Southern California, via CIRM
View Media
3272: Ear hair cells derived from embryonic stem cells
3272: Ear hair cells derived from embryonic stem cells
Mouse embryonic stem cells matured into this bundle of hair cells similar to the ones that transmit sound in the ear. These cells could one day be transplanted as a therapy for some forms of deafness, or they could be used to screen drugs to treat deafness. The hairs are shown at 23,000 times magnification via scanning electron microscopy. Image and caption information courtesy of the California Institute for Regenerative Medicine.
Stefen Heller, Stanford University, via CIRM
View Media
3459: Structure of telomerase
3459: Structure of telomerase
Scientists recently discovered the full molecular structure of telomerase, an enzyme important to aging and cancer. Within each cell, telomerase maintains the telomeres, or end pieces, of a chromosome, preserving genetic data and extending the life of the cell. In their study, a team from UCLA and UC Berkeley found the subunit p50, shown in red, to be a keystone in the enzyme's structure and function. Featured in the May 16, 2013 issue of Biomedical Beat.
Jiansen Jiang, Edward J. Miracco, Z. Hong Zhou and Juli Feigon, University of California, Los Angeles; Kathleen Collins, University of California, Berkeley
View Media
3374: Electrostatic map of the adeno-associated virus
3374: Electrostatic map of the adeno-associated virus
The new highly efficient parallelized DelPhi software was used to calculate the potential map distribution of an entire virus, the adeno-associated virus, which is made up of more than 484,000 atoms. Despite the relatively large dimension of this biological system, resulting in 815x815x815 mesh points, the parallelized DelPhi, utilizing 100 CPUs, completed the calculations within less than three minutes. Related to image 3375.
Emil Alexov, Clemson University
View Media
6572: Nuclear Lamina
6572: Nuclear Lamina
The 3D single-molecule super-resolution reconstruction of the entire nuclear lamina in a HeLa cell was acquired using the TILT3D platform. TILT3D combines a tilted light sheet with point-spread function (PSF) engineering to provide a flexible imaging platform for 3D single-molecule super-resolution imaging in mammalian cells.
See 6573 for 3 separate views of this structure.
See 6573 for 3 separate views of this structure.
Anna-Karin Gustavsson, Ph.D.
View Media
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)
View Media
3735: Scanning electron microscopy of collagen fibers
3735: Scanning electron microscopy of collagen fibers
This image shows collagen, a fibrous protein that's the main component of the extracellular matrix (ECM). Collagen is a strong, ropelike molecule that forms stretch-resistant fibers. The most abundant protein in our bodies, collagen accounts for about a quarter of our total protein mass. Among its many functions is giving strength to our tendons, ligaments and bones and providing scaffolding for skin wounds to heal. There are about 20 different types of collagen in our bodies, each adapted to the needs of specific tissues.
Tom Deerinck, National Center for Microscopy and Imaging Research (NCMIR)
View Media
2332: Tiny points of light in a quantum dot
2332: Tiny points of light in a quantum dot
This fingertip-shaped group of lights is a microscopic crystal called a quantum dot. About 10,000 times thinner than a sheet of paper, the dot radiates brilliant colors under ultraviolet light. Dots such as this one allow researchers to label and track individual molecules in living cells and may be used for speedy disease diagnosis, DNA testing, and screening for illegal drugs.
Sandra Rosenthal and James McBride, Vanderbilt University, and Stephen Pennycook, Oak Ridge National Laboratory
View Media
2529: Aspirin
2529: Aspirin
Acetylsalicylate (bottom) is the aspirin of today. Adding a chemical tag called an acetyl group (shaded box, bottom) to a molecule derived from willow bark (salicylate, top) makes the molecule less acidic (and easier on the lining of the digestive tract), but still effective at relieving pain. See image 2530 for a labeled version of this illustration. Featured in Medicines By Design.
Crabtree + Company
View Media
3386: HIV Infected Cell
3386: HIV Infected Cell
The human immunodeficiency virus (HIV), shown here as tiny purple spheres, causes the disease known as AIDS (for acquired immunodeficiency syndrome). HIV can infect multiple cells in your body, including brain cells, but its main target is a cell in the immune system called the CD4 lymphocyte (also called a T-cell or CD4 cell).
Tom Deerinck, National Center for Microscopy and Imaging Research (NCMIR)
View Media
6344: Drosophila
6344: Drosophila
Two adult fruit flies (Drosophila)
Dr. Vicki Losick, MDI Biological Laboratory, www.mdibl.org
View Media
3771: Molecular model of freshly made Rous sarcoma virus (RSV)
3771: Molecular model of freshly made Rous sarcoma virus (RSV)
Viruses have been the foes of animals and other organisms for time immemorial. For almost as long, they've stayed well hidden from view because they are so tiny (they aren't even cells, so scientists call the individual virus a "particle"). This image shows a molecular model of a particle of the Rous sarcoma virus (RSV), a virus that infects and sometimes causes cancer in chickens. In the background is a photo of red blood cells. The particle shown is "immature" (not yet capable of infecting new cells) because it has just budded from an infected chicken cell and entered the bird's bloodstream. The outer shell of the immature virus is made up of a regular assembly of large proteins (shown in red) that are linked together with short protein molecules called peptides (green). This outer shell covers and protects the proteins (blue) that form the inner shell of the particle. But as you can see, the protective armor of the immature virus contains gaping holes. As the particle matures, the short peptides are removed and the large proteins rearrange, fusing together into a solid sphere capable of infecting new cells. While still immature, the particle is vulnerable to drugs that block its development. Knowing the structure of the immature particle may help scientists develop better medications against RSV and similar viruses in humans. Scientists used sophisticated computational tools to reconstruct the RSV atomic structure by crunching various data on the RSV proteins to simulate the entire structure of immature RSV.
Boon Chong Goh, University of Illinois at Urbana-Champaign
View Media
2561: Histones in chromatin (with labels)
2561: Histones in chromatin (with labels)
Histone proteins loop together with double-stranded DNA to form a structure that resembles beads on a string. See image 2560 for an unlabeled version of this illustration. Featured in The New Genetics.
Crabtree + Company
View Media
1102: Endothelial cell
1102: Endothelial cell
This image shows two components of the cytoskeleton, microtubules (green) and actin filaments (red), in an endothelial cell derived from a cow lung. The cystoskeleton provides the cell with an inner framework and enables it to move and change shape.
Tina Weatherby Carvalho, University of Hawaii at Manoa
View Media
1247: Crab nerve cell
1247: Crab nerve cell
Neuron from a crab showing the cell body (bottom), axon (rope-like extension), and growth cone (top right).
Tina Weatherby Carvalho, University of Hawaii at Manoa
View Media