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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.

5730: Dynamic cryo-EM model of the human transcription preinitiation complex
5730: Dynamic cryo-EM model of the human transcription preinitiation complex
Gene transcription is a process by which 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 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. This animation shows the different TFIID components as they contact DNA and recruit the RNA polymerase for gene transcription.
To learn more about the research that has shed new light on gene transcription, see this news release from Berkeley Lab.
Related to image 3766.
To learn more about the research that has shed new light on gene transcription, see this news release from Berkeley Lab.
Related to image 3766.
Eva Nogales, Berkeley Lab
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6788: Mitosis and meiosis compared-labeled
6788: Mitosis and meiosis compared-labeled
Meiosis is used to make sperm and egg cells. During meiosis, a cell's chromosomes are copied once, but the cell divides twice. During mitosis, the chromosomes are copied once, and the cell divides once. For simplicity, cells are illustrated with only three pairs of chromosomes.
See image 1333 for an unlabeled version of this illustration.
See image 1333 for an unlabeled version of this illustration.
Judith Stoffer
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3403: Disrupted vascular development in frog embryos
3403: Disrupted vascular development in frog embryos
Disassembly of vasculature in kdr:GFP frogs following addition of 250 µM TBZ. Related to images 3404 and 3505.
Hye Ji Cha, University of Texas at Austin
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5772: Confocal microscopy image of two Drosophila ovarioles
5772: Confocal microscopy image of two Drosophila ovarioles
Ovarioles in female insects are tubes in which egg cells (called oocytes) form at one end and complete their development as they reach the other end of the tube. This image, taken with a confocal microscope, shows ovarioles in a very popular lab animal, the fruit fly Drosophila. The basic structure of ovarioles supports very rapid egg production, with some insects (like termites) producing several thousand eggs per day. Each insect ovary typically contains four to eight ovarioles, but this number varies widely depending on the insect species.
Scientists use insect ovarioles, for example, to study the basic processes that help various insects, including those that cause disease (like some mosquitos and biting flies), reproduce very quickly.
Scientists use insect ovarioles, for example, to study the basic processes that help various insects, including those that cause disease (like some mosquitos and biting flies), reproduce very quickly.
2004 Olympus BioScapes Competition
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2453: Seeing signaling protein activation in cells 03
2453: Seeing signaling protein activation in cells 03
Cdc42, a member of the Rho family of small guanosine triphosphatase (GTPase) proteins, regulates multiple cell functions, including motility, proliferation, apoptosis, and cell morphology. In order to fulfill these diverse roles, the timing and location of Cdc42 activation must be tightly controlled. Klaus Hahn and his research group use special dyes designed to report protein conformational changes and interactions, here in living neutrophil cells. Warmer colors in this image indicate higher levels of activation. Cdc42 looks to be activated at cell protrusions.
Related to images 2451, 2452, and 2454.
Related to images 2451, 2452, and 2454.
Klaus Hahn, University of North Carolina, Chapel Hill Medical School
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3753: Coronavirus spike protein structure
3753: Coronavirus spike protein structure
Coronaviruses are enveloped viruses responsible for 30 percent of mild respiratory infections and atypical deadly pneumonia in humans worldwide. These deadly pneumonia include those caused by infections with severe acute respiratory syndrome coronavirus (SARS-CoV) and Middle East respiratory syndrome coronavirus (MERS-CoV). The coronavirus spike glycoprotein mediates virus entry into cells and represents an important therapeutic target. The illustration shows a viral membrane decorated with spike glycoproteins; highlighted in red is a potential neutralization site, which is a protein sequence that might be used as a target for vaccines to combat viruses such as MERS-CoV and other coronaviruses.
Melody Campbell, UCSF
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3362: Sphingolipid S1P1 receptor
3362: Sphingolipid S1P1 receptor
The receptor is shown bound to an antagonist, ML056.
Raymond Stevens, The Scripps Research Institute
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6808: Fruit fly larvae brains showing tubulin
6808: Fruit fly larvae brains showing tubulin
Two fruit fly (Drosophila melanogaster) larvae brains with neurons expressing fluorescently tagged tubulin protein. Tubulin makes up strong, hollow fibers called microtubules that play important roles in neuron growth and migration during brain development. This image was captured using confocal microscopy, and the color indicates the position of the neurons within the brain.
Vladimir I. Gelfand, Feinberg School of Medicine, Northwestern University.
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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.
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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
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2350: Mandelate racemase from B. subtilis
2350: Mandelate racemase from B. subtilis
Model of the mandelate racemase enzyme from Bacillus subtilis, a bacterium commonly found in soil.
New York Structural GenomiX Research Consortium, PSI
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2758: Cross section of a Drosophila melanogaster pupa
2758: Cross section of a Drosophila melanogaster pupa
This photograph shows a magnified view of a Drosophila melanogaster pupa in cross section. Compare this normal pupa to one that lacks an important receptor, shown in image 2759.
Christina McPhee and Eric Baehrecke, University of Massachusetts Medical School
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3718: A Bacillus subtilis biofilm grown in a Petri dish
3718: A Bacillus subtilis biofilm grown in a Petri dish
Bacterial biofilms are tightly knit communities of bacterial cells growing on, for example, solid surfaces, such as in water pipes or on teeth. Here, cells of the bacterium Bacillus subtilis have formed a biofilm in a laboratory culture. Researchers have discovered that the bacterial cells in a biofilm communicate with each other through electrical signals via specialized potassium ion channels to share resources, such as nutrients, with each other. This insight may help scientists to improve sanitation systems to prevent biofilms, which often resist common treatments, from forming and to develop better medicines to combat bacterial infections. See the Biomedical Beat blog post Bacterial Biofilms: A Charged Environment for more information.
Gürol Süel, UCSD
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6762: CCP enzyme
6762: CCP enzyme
The enzyme CCP is found in the mitochondria of baker’s yeast. Scientists study the chemical reactions that CCP triggers, which involve a water molecule, iron, and oxygen. This structure was determined using an X-ray free electron laser.
Protein Data Bank.
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6489: CRISPR Illustration Frame 5
6489: CRISPR Illustration Frame 5
This illustration shows, in simplified terms, how the CRISPR-Cas9 system can be used as a gene-editing tool. This is the fifthframe in a series of five. The CRISPR system has two components joined together: a finely tuned targeting device (a small strand of RNA programmed to look for a specific DNA sequence) and a strong cutting device (an enzyme called Cas9 that can cut through a double strand of DNA). For an explanation and overview of the CRISPR-Cas9 system, see the NIGMS Biomedical Beat blog entry, Field Focus: Precision Gene Editing with CRISPR and the iBiology video, Genome Engineering with CRISPR-Cas9: Birth of a Breakthrough Technology.
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5753: Clathrin-mediated endocytosis
5753: Clathrin-mediated endocytosis
Endocytosis is the process by which cells are able to take up membrane and extracellular materials through the formation of a small intracellular bubble, called a vesicle. This process, called membrane budding, is generally by a coating of proteins. This protein coat helps both to deform the membrane and to concentrate specific proteins inside the newly forming vesicle. Clathrin is a coat protein that functions in receptor-mediated endocytosis events at the plasma membrane. This animation shows the process of clathrin-mediated endocytosis. An iron-transport protein called transferrin (blue) is bound to its receptor (purple) on the exterior cell membrane. Inside the cell, a clathrin cage (shown in white/beige) assembles through interactions with membrane-bound adaptor proteins (green), causing the cell membrane to begin bending. The adaptor proteins also bind to receptors for transferrin, capturing them in the growing vesicle. Molecules of a protein called dynamin (purple) are then recruited to the neck of the vesicle and are involved in separating the membranes of the cell and the vesicle. Soon after the vesicle has budded off the membrane, the clathrin cage is disassembled. This disassembly is mediated by another protein called HSC70 (yellow), and its cofactor protein auxilin (orange).
Janet Iwasa, University of Utah
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2566: Haplotypes
2566: Haplotypes
Haplotypes are combinations of gene variants that are likely to be inherited together within the same chromosomal region. In this example, an original haplotype (top) evolved over time to create three newer haplotypes that each differ by a few nucleotides (red). See image 2567 for a labeled version of this illustration. Featured in The New Genetics.
Crabtree + Company
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5779: Microsporidia in roundworm 3
5779: Microsporidia in roundworm 3
Many disease-causing microbes manipulate their host’s metabolism and cells for their own ends. Microsporidia—which are parasites closely related to fungi—infect and multiply inside animal cells, and take the rearranging of cells’ interiors to a new level. They reprogram animal cells such that the cells start to fuse, causing them to form long, continuous tubes. As shown in this image of the roundworm Caenorhabditis elegans, microsporidia (shown in red) have invaded the worm’s gut cells (the large blue dots are the cells' nuclei) and have instructed the cells to merge. The cell fusion enables the microsporidia to thrive and propagate in the expanded space. Scientists study microsporidia in worms to gain more insight into how these parasites manipulate their host cells. This knowledge might help researchers devise strategies to prevent or treat infections with microsporidia.
For more on the research into microsporidia, see this news release from the University of California San Diego. Related to images 5777 and 5778.
For more on the research into microsporidia, see this news release from the University of California San Diego. Related to images 5777 and 5778.
Keir Balla and Emily Troemel, University of California San Diego
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2410: DNase
2410: DNase
Crystals of DNase protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.
Alex McPherson, University of California, Irvine
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3730: A molecular interaction network in yeast 1
3730: A molecular interaction network in yeast 1
The image visualizes a part of the yeast molecular interaction network. The lines in the network represent connections among genes (shown as little dots) and different-colored networks indicate subnetworks, for instance, those in specific locations or pathways in the cell. Researchers use gene or protein expression data to build these networks; the network shown here was visualized with a program called Cytoscape. By following changes in the architectures of these networks in response to altered environmental conditions, scientists can home in on those genes that become central "hubs" (highly connected genes), for example, when a cell encounters stress. They can then further investigate the precise role of these genes to uncover how a cell's molecular machinery deals with stress or other factors. Related to images 3732 and 3733.
Keiichiro Ono, UCSD
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6897: Zebrafish embryo
6897: Zebrafish embryo
A zebrafish embryo showing its natural colors. Zebrafish have see-through eggs and embryos, making them ideal research organisms for studying the earliest stages of development. This image was taken in transmitted light under a polychromatic polarizing microscope.
Michael Shribak, Marine Biological Laboratory/University of Chicago.
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2523: Plasma membrane
2523: Plasma membrane
The plasma membrane is a cell's protective barrier. See image 2524 for a labeled version of this illustration. Featured in The Chemistry of Health.
Crabtree + Company
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6522: Fruit fly ovary
6522: Fruit fly ovary
In this image of a stained fruit fly ovary, the ovary is packed with immature eggs (with DNA stained blue). The cytoskeleton (in pink) is a collection of fibers that gives a cell shape and support. The signal-transmitting molecules like STAT (in yellow) are common to reproductive processes in humans. Researchers used this image to show molecular staining and high-resolution imaging techniques to students.
Crystal D. Rogers, Ph.D., University of California, Davis, School of Veterinary Medicine; and Mariano A. Loza-Coll, Ph.D., California State University, Northridge.
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6355: H1N1 Influenza Virus
6355: H1N1 Influenza Virus
CellPack image of the H1N1 influenza virus, with hemagglutinin and neuraminidase glycoproteins in green and red, respectively, on the outer envelope (white); matrix protein in gray, and ribonucleoprotein particles inside the virus in red and green. Related to image 6356.
Dr. Rommie Amaro, University of California, San Diego
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3733: A molecular interaction network in yeast 3
3733: A molecular interaction network in yeast 3
The image visualizes a part of the yeast molecular interaction network. The lines in the network represent connections among genes (shown as little dots) and different-colored networks indicate subnetworks, for instance, those in specific locations or pathways in the cell. Researchers use gene or protein expression data to build these networks; the network shown here was visualized with a program called Cytoscape. By following changes in the architectures of these networks in response to altered environmental conditions, scientists can home in on those genes that become central "hubs" (highly connected genes), for example, when a cell encounters stress. They can then further investigate the precise role of these genes to uncover how a cell's molecular machinery deals with stress or other factors. Related to images 3730 and 3732.
Keiichiro Ono, UCSD
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2684: Dicty fruit
2684: Dicty fruit
Dictyostelium discoideum is a microscopic amoeba. A group of 100,000 form a mound as big as a grain of sand. Featured in The New Genetics.
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3486: Apoptosis reversed
3486: Apoptosis reversed
Two healthy cells (bottom, left) enter into apoptosis (bottom, center) but spring back to life after a fatal toxin is removed (bottom, right; top).
Hogan Tang of the Denise Montell Lab, Johns Hopkins University School of Medicine
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2402: RNase A (2)
2402: RNase A (2)
A crystal of RNase A protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.
Alex McPherson, University of California, Irvine
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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.
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6547: Cell Nucleus and Lipid Droplets
6547: Cell Nucleus and Lipid Droplets
A cell nucleus (blue) surrounded by lipid droplets (yellow). Exogenously expressed, S-tagged UBXD8 (green) recruits endogenous p97/VCP (red) to the surface of lipid droplets in oleate-treated HeLa cells. Nucleus stained with DAPI.
James Olzmann, University of California, Berkeley
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3451: Proteasome
3451: Proteasome
This fruit fly spermatid recycles various molecules, including malformed or damaged proteins. Actin filaments (red) in the cell draw unwanted proteins toward a barrel-shaped structure called the proteasome (green clusters), which degrades the molecules into their basic parts for re-use.
Sigi Benjamin-Hong, Rockefeller University
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3252: Neural circuits in worms similar to those in humans
3252: Neural circuits in worms similar to those in humans
Green and yellow fluorescence mark the processes and cell bodies of some C. elegans neurons. Researchers have found that the strategies used by this tiny roundworm to control its motions are remarkably similar to those used by the human brain to command movement of our body parts. From a November 2011 University of Michigan news release.
Shawn Xu, University of Michigan
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6356: H1N1 Influenza Virus
6356: H1N1 Influenza Virus
Related to image 6355.
Dr. Rommie Amaro, University of California, San Diego
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3277: Human ES cells turn into insulin-producing cells
3277: Human ES cells turn into insulin-producing cells
Human embryonic stem cells were differentiated into cells like those found in the pancreas (blue), which give rise to insulin-producing cells (red). When implanted in mice, the stem cell-derived pancreatic cells can replace the insulin that isn't produced in type 1 diabetes. Image and caption information courtesy of the California Institute for Regenerative Medicine.
Eugene Brandon, ViaCyte, via CIRM
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3326: Cytochrome structure with anticancer drug
3326: Cytochrome structure with anticancer drug
This image shows the structure of the CYP17A1 enzyme (ribbons colored from blue N-terminus to red C-terminus), with the associated heme colored black. The prostate cancer drug abiraterone is colored gray. Cytochrome P450 enzymes bind to and metabolize a variety of chemicals, including drugs. Cytochrome P450 17A1 also helps create steroid hormones. Emily Scott's lab is studying how CYP17A1 could be selectively inhibited to treat prostate cancer. She and graduate student Natasha DeVore elucidated the structure shown using X-ray crystallography. Dr. Scott created the image (both white bg and transparent bg) for the NIGMS image gallery. See the "Medium-Resolution Image" for a PNG version of the image that is transparent.
Emily Scott, University of Kansas
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3491: Kinesin moves cellular cargo
3491: Kinesin moves cellular cargo
A protein called kinesin (blue) is in charge of moving cargo around inside cells and helping them divide. It's powered by biological fuel called ATP (bright yellow) as it scoots along tube-like cellular tracks called microtubules (gray).
Charles Sindelar, Yale University
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3677: Human skeletal muscle
3677: Human skeletal muscle
Cross section of human skeletal muscle. Image taken with a confocal fluorescent light microscope.
Tom Deerinck, National Center for Microscopy and Imaging Research (NCMIR)
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2542: Nucleotides make up DNA (with labels)
2542: Nucleotides make up DNA (with labels)
DNA consists of two long, twisted chains made up of nucleotides. Each nucleotide contains one base, one phosphate molecule, and the sugar molecule deoxyribose. The bases in DNA nucleotides are adenine, thymine, cytosine, and guanine. See image 2541 for an unlabeled version of this illustration. Featured in The New Genetics.
Crabtree + Company
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3395: NCMIR mouse tail
3395: NCMIR mouse tail
Stained cross section of a mouse tail.
Tom Deerinck, National Center for Microscopy and Imaging Research (NCMIR)
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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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6534: Mosaicism in C. elegans (White Background)
6534: Mosaicism in C. elegans (White Background)
In the worm C. elegans, double-stranded RNA made in neurons can silence matching genes in a variety of cell types through the transport of RNA between cells. The head region of three worms that were genetically modified to express a fluorescent protein were imaged and the images were color-coded based on depth. The worm on the left lacks neuronal double-stranded RNA and thus every cell is fluorescent. In the middle worm, the expression of the fluorescent protein is silenced by neuronal double-stranded RNA and thus most cells are not fluorescent. The worm on the right lacks an enzyme that amplifies RNA for silencing. Surprisingly, the identities of the cells that depend on this enzyme for gene silencing are unpredictable. As a result, worms of identical genotype are nevertheless random mosaics for how the function of gene silencing is carried out. For more, see journal article and press release. Related to image 6532.
Snusha Ravikumar, Ph.D., University of Maryland, College Park, and Antony M. Jose, Ph.D., University of Maryland, College Park
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6773: Endoplasmic reticulum abnormalities
6773: Endoplasmic reticulum abnormalities
Human cells with the gene that codes for the protein FIT2 deleted. Green indicates an endoplasmic reticulum (ER) resident protein. The lack of FIT2 affected the structure of the ER and caused the resident protein to cluster in ER membrane aggregates, seen as large, bright-green spots. Red shows where the degradation of cell parts—called autophagy—is taking place, and the nucleus is visible in blue. This image was captured using a confocal microscope.
Michel Becuwe, Harvard University.
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5815: Introduction to Genome Editing Using CRISPR/Cas9
5815: Introduction to Genome Editing Using CRISPR/Cas9
Genome editing using CRISPR/Cas9 is a rapidly expanding field of scientific research with emerging applications in disease treatment, medical therapeutics and bioenergy, just to name a few. This technology is now being used in laboratories all over the world to enhance our understanding of how living biological systems work, how to improve treatments for genetic diseases and how to develop energy solutions for a better future.
Janet Iwasa
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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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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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2488: VDAC-1 (1)
2488: VDAC-1 (1)
The structure of the pore-forming protein VDAC-1 from humans. This molecule mediates the flow of products needed for metabolism--in particular the export of ATP--across the outer membrane of mitochondria, the power plants for eukaryotic cells. VDAC-1 is involved in metabolism and the self-destruction of cells--two biological processes central to health.
Related to images 2491, 2494, and 2495.
Related to images 2491, 2494, and 2495.
Gerhard Wagner, Harvard Medical School
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2347: Cysteine dioxygenase from mouse
2347: Cysteine dioxygenase from mouse
Model of the mammalian iron enzyme cysteine dioxygenase from a mouse.
Center for Eukaryotic Structural Genomics, PSI
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3782: A multicolored fish scale 1
3782: A multicolored fish scale 1
Each of the colored specs in this image is a cell on the surface of a fish scale. To better understand how wounds heal, scientists have inserted genes that make cells brightly glow in different colors into the skin cells of zebrafish, a fish often used in laboratory research. The colors enable the researchers to track each individual cell, for example, as it moves to the location of a cut or scrape over the course of several days. These technicolor fish endowed with glowing skin cells dubbed "skinbow" provide important insight into how tissues recover and regenerate after an injury.
For more information on skinbow fish, see the Biomedical Beat blog post Visualizing Skin Regeneration in Real Time and a press release from Duke University highlighting this research. Related to image 3783.
For more information on skinbow fish, see the Biomedical Beat blog post Visualizing Skin Regeneration in Real Time and a press release from Duke University highlighting this research. Related to image 3783.
Chen-Hui Chen and Kenneth Poss, Duke University
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3396: Myelinated axons 1
3396: Myelinated axons 1
Myelinated axons in a rat spinal root. Myelin is a type of fat that forms a sheath around and thus insulates the axon to protect it from losing the electrical current needed to transmit signals along the axon. The axoplasm inside the axon is shown in pink. Related to 3397.
Tom Deerinck, National Center for Microscopy and Imaging Research (NCMIR)
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5767: Multivesicular bodies containing intralumenal vesicles assemble at the vacuole 3
5767: Multivesicular bodies containing intralumenal vesicles assemble at the vacuole 3
Collecting and transporting cellular waste and sorting it into recylable and nonrecylable pieces is a complex business in the cell. One key player in that process is the endosome, which helps collect, sort and transport worn-out or leftover proteins with the help of a protein assembly called the endosomal sorting complexes for transport (or ESCRT for short). These complexes help package proteins marked for breakdown into intralumenal vesicles, which, in turn, are enclosed in multivesicular bodies for transport to the places where the proteins are recycled or dumped. In this image, two multivesicular bodies (with yellow membranes) contain tiny intralumenal vesicles (with a diameter of only 25 nanometers; shown in red) adjacent to the cell's vacuole (in orange).
Scientists working with baker's yeast (Saccharomyces cerevisiae) study the budding inward of the limiting membrane (green lines on top of the yellow lines) into the intralumenal vesicles. This tomogram was shot with a Tecnai F-20 high-energy electron microscope, at 29,000x magnification, with a 0.7-nm pixel, ~4-nm resolution.
To learn more about endosomes, see the Biomedical Beat blog post The Cell’s Mailroom. Related to a microscopy photograph 5768 that was used to generate this illustration and a zoomed-out version 5769 of this illustration.
Scientists working with baker's yeast (Saccharomyces cerevisiae) study the budding inward of the limiting membrane (green lines on top of the yellow lines) into the intralumenal vesicles. This tomogram was shot with a Tecnai F-20 high-energy electron microscope, at 29,000x magnification, with a 0.7-nm pixel, ~4-nm resolution.
To learn more about endosomes, see the Biomedical Beat blog post The Cell’s Mailroom. Related to a microscopy photograph 5768 that was used to generate this illustration and a zoomed-out version 5769 of this illustration.
Matthew West and Greg Odorizzi, University of Colorado
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