Like a map showing heavily traveled roads, this mathematical model of metabolic activity inside an E. coli cell shows the busiest pathway in white. Reaction pathways used less frequently by the cell are marked in red (moderate activity) and green (even less activity). Visualizations like this one may help scientists identify drug targets that block key metabolic pathways in bacteria.

Vibrio, a type (genus) of rod-shaped bacteria. Some Vibrio species cause cholera in humans.

Genes are often interrupted by stretches of DNA (introns, blue) that do not contain instructions for making a protein. The DNA segments that do contain protein-making instructions are known as exons (green). See image 2550 for an unlabeled version of this illustration. Featured in The New Genetics.

Hydra magnipapillata is an invertebrate animal used as a model organism to study developmental questions, for example the formation of the body axis.

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.

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 are starting to separate to form two new cells.

NIGMS staff are located in the Natcher Building on the NIH campus.

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.

Structure of the bacterial antitoxin protein GhoS. GhoS inhibits the production of a bacterial toxin, GhoT, which can contribute to antibiotic resistance. GhoS is the first known bacterial antitoxin that works by cleaving the messenger RNA that carries the instructions for making the toxin. More information can be found in the paper: Wang X, Lord DM, Cheng HY, Osbourne DO, Hong SH, Sanchez-Torres V, Quiroga C, Zheng K, Herrmann T, Peti W, Benedik MJ, Page R, Wood TK. A new type V toxin-antitoxin system where mRNA for toxin GhoT is cleaved by antitoxin GhoS. Nat Chem Biol. 2012 Oct;8(10):855-61. Related to 3427.

Relapsing fever is caused by a bacterium and transmitted by certain soft-bodied ticks or body lice. The disease is seldom fatal in humans, but it can be very serious and prolonged. This scanning electron micrograph shows Borrelia hermsii (green), one of the bacterial species that causes the disease, interacting with red blood cells. Micrograph by Robert Fischer, NIAID. Related to image 3586.
For more information about relapsing fever, see https://www.cdc.gov/relapsing-fever/index.html.
This image is part of the Life: Magnified collection, which was displayed in the Gateway Gallery at Washington Dulles International Airport June 3, 2014, to January 21, 2015.

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.

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.

Sulfite oxidase is an enzyme that is essential for normal neurological development in children. This video shows the active site of the enzyme and its molybdenum cofactor visible as a faint ball-and-stick representation buried within the protein. The positively charged channel (blue) at the active site contains a chloride ion (green) and three water molecules (red). As the protein oscillates, one can see directly down the positively charged channel. At the bottom is the molybdenum atom of the active site (light blue) and its oxo group (red) that is transferred to sulfite to form sulfate in the catalytic reaction.

Macrophages (green) are the professional eaters of our immune system. They are constantly surveilling our tissues for targets—such as bacteria, dead cells, or even cancer—and clearing them before they can cause harm. In this image, researchers were testing how macrophages responded to different molecules that were attached to silica beads (magenta) coated with a lipid bilayer to mimic a cell membrane.

Find more information on this image in the NIH Director’s Blog post "How to Feed a Macrophage."

The feeding tube, or pharynx, of a planarian worm with cilia shown in red and muscle fibers shown in green

This is a fibroblast, a connective tissue cell that plays an important role in wound healing. Normal fibroblasts have smooth edges. In contrast, this spiky cell is missing a protein that is necessary for proper construction of the cell's skeleton. Its jagged shape makes it impossible for the cell to move normally. In addition to compromising wound healing, abnormal cell movement can lead to birth defects, faulty immune function, and other health problems.

This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.

Arranging exons in different patterns, called alternative splicing, enables cells to make different proteins from a single gene. Featured in The New Genetics.

See image 2552 for an unlabeled version of this illustration.

In this image, recombinant probes known as FingRs (Fibronectin Intrabodies Generated by mRNA display) were expressed in a cortical neuron, where they attached fluorescent proteins to either PSD95 (green) or Gephyrin (red). PSD-95 is a marker for synaptic strength at excitatory postsynaptic sites, and Gephyrin plays a similar role at inhibitory postsynaptic sites. Thus, using FingRs it is possible to obtain a map of synaptic connections onto a particular neuron in a living cell in real time.

X-ray crystallography allows researchers to see structures too small to be seen by even the most powerful microscopes. To visualize the arrangement of atoms within molecules, researchers can use the diffraction patterns obtained by passing X-ray beams through crystals of the molecule. This is a common way for solving the structures of proteins. See image 2511 for an unlabeled version of this illustration. Featured in The Structures of Life.

The intense X-rays produced by synchrotrons such as the Advanced Photon Source are ideally suited for protein structure determination. Using synchrotron X-rays and advanced computers scientists can determine protein structures at a pace unheard of decades ago.

Mosquito larvae with genes edited by CRISPR. This species of mosquito, Culex quinquefasciatus, can transmit West Nile virus, Japanese encephalitis virus, and avian malaria, among other diseases. The researchers who took this image developed a gene-editing toolkit for Culex quinquefasciatus that could ultimately help stop the mosquitoes from spreading pathogens. The work is described in the Nature Communications paper "Optimized CRISPR tools and site-directed transgenesis towards gene drive development in Culex quinquefasciatus mosquitoes" by Feng et al. Related to image 6769 and video 6771.

The arrangement of identical molecular components can make a dramatic difference. For example, carbon atoms can be arranged into dull graphite (left) or sparkly diamonds (right). See image 2506 for an illustration without examples.

It has been said that gastrulation is the most important event in a person's life. This part of early embryonic development transforms a simple ball of cells and begins to define cell fate and the body axis. In a study published in Science magazine in March 2012, NIGMS grantee Bob Goldstein and his research group studied how contractions of actomyosin filaments in C. elegans and Drosophila embryos lead to dramatic rearrangements of cell and embryonic structure. This research is described in detail in the following article: "Triggering a Cell Shape Change by Exploiting Preexisting Actomyosin Contractions." In these images, myosin (green) and plasma membrane (red) are highlighted at four timepoints in gastrulation in the roundworm C. elegans. The blue highlights in the top three frames show how cells are internalized, and the site of closure around the involuting cells is marked with an arrow in the last frame. See related video 3334.

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, a multivesicular body (the round structure slightly to the right of center) contain tiny intralumenal vesicles (with a diameter of only 25 nanometers; the round specks inside the larger round structure) adjacent to the cell's vacuole (below the multivesicular body, shown in darker and more uniform gray).

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 color-enhanced version 5767 and image 5769.

This video shows 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 videos 2570 and 2571.

Hippocampal neuron from rodent brain with dendrites shown in blue. The hundreds of tiny magenta, green and white dots are the dendritic spines of excitatory synapses.

A rendering of an activity biosensor image overlaid with a cell-centered frame of reference used for image analysis of signal transduction. This is an example of NIH-supported research on single-cell analysis. Related to 2798 , 2799, 2800, 2801 and 2803.

On top, the brain of a sleep-deprived fly glows orange because of Bruchpilot, a communication protein between brain cells. These bright orange brain areas are associated with learning. On the bottom, a well-rested fly shows lower levels of Bruchpilot, which might make the fly ready to learn after a good night's rest.

Damage to each person's genome, often called the "Book of Life," accumulates with time. Such DNA mutations arise from errors in the DNA copying process, as well as from external sources, such as sunlight and cigarette smoke. DNA mutations are known to cause cancer and also may contribute to cellular aging.

These vials may look like they're filled with colored water, but they really contain nanocrystals reflecting different colors under ultraviolet light. The tiny crystals, made of semiconducting compounds, are called quantum dots. Depending on their size, the dots emit different colors that let scientists use them as a tool for detecting particular genes, proteins, and other biological molecules.

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 labeled version of this illustration and 2549 for a labeled and numbered version. Featured in The New Genetics.

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.

Here, a human HeLa cell (a type of immortal cell line used in laboratory experiments) is undergoing cell division. They come from cervical cancer cells that were obtained in 1951 from Henrietta Lacks, a patient at the Johns Hopkins Hospital. The final stage of division, called cytokinesis, occurs after the genomes—shown in yellow—have split into two new daughter cells. The myosin II is a motor protein shown in blue, and the actin filaments, which are types of protein that support cell structure, are shown in red.

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 are separating to form the cores of two new cells.

Related to images 1011, 1012, 1013, 1014, 1015, 1016, 1017, 1018, 1019, and 1021.

A Trigonium diatom imaged by a quantitative orientation-independent differential interference contrast (OI-DIC) microscope. Diatoms are single-celled photosynthetic algae with mineralized cell walls that contain silica and provide protection and support. These organisms form an important part of the plankton at the base of the marine and freshwater food chains. The width of this image is 90 μm.

More information about the microscopy that produced this image can be found in the Journal of Microscopy paper “An Orientation-Independent DIC Microscope Allows High Resolution Imaging of Epithelial Cell Migration and Wound Healing in a Cnidarian Model” by Malamy and Shribak.

The microtubule severing protein, katanin, localizes to chromosomes and regulates anaphase A in mitosis. The movement of chromosomes on the mitotic spindle requires the depolymerization of microtubule ends. The figure shows the mitotic localization of the microtubule severing protein katanin (green) relative to spindle microtubules (red) and kinetochores/chromosomes (blue). Katanin targets to chromosomes during both metaphase (top) and anaphase (bottom) and is responsible for inducing the depolymerization of attached microtubule plus-ends. This image was a finalist in the 2008 Drosophila Image Award.

Duplicated pair of chromosomes have exchanged material.

A crystal of pig trypsin protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.

A crystal of bacterial glucose isomerase protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.

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 3374.

Crystals of bovine milk alpha-lactalbumin protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.

This network map shows the overlap (green) between the long QT syndrome (yellow) and epilepsy (blue) protein-interaction neighborhoods located within the human interactome. Researchers have learned to integrate genetic, cellular and clinical information to find out why certain medicines can trigger fatal heart arrhythmias. Featured in Computing Life magazine.

An image of the area of the mouse brain that serves as the 'master clock,' which houses the brain's time-keeping neurons. The nuclei of the clock cells are shown in blue. A small molecule called VIP, shown in green, enables neurons in the central clock in the mammalian brain to synchronize.

Kinases are enzymes that add phosphate groups (red-yellow structures) to proteins (green), assigning the proteins a code. In this reaction, an intermediate molecule called ATP (adenosine triphosphate) donates a phosphate group from itself, becoming ADP (adenosine diphosphate). See image 2534 for an unlabeled version of this illustration. Featured in Medicines By Design.

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.

A sensor particle being engulfed by a macrophage—an immune cell—and encapsuled in a compartment called a phagosome. The phagosome then fuses with lysosomes—another type of compartment. The left video shows snowman-shaped sensor particles with fluorescent green nanoparticle “heads” and “bodies” colored red by Förster Resonance Energy Transfer (FRET)-donor fluorophores. The middle video visualizes light blue FRET signals that are only generated when the “snowman” sensor—the FRET-donor—fuses with the lysosomes, which are loaded with FRET-acceptors. The right video combines the other two. The videos were captured using epi-fluorescence microscopy.

More details can be found in the paper “Transport motility of phagosomes on actin and microtubules regulates timing and kinetics of their maturation” by Yu et al.

Crystal structure of the beta2-adrenergic receptor protein. This is the first known structure of a human G protein-coupled receptor, a large family of proteins that control critical bodily functions and the action of about half of today's pharmaceuticals. Featured as one of the November 2007 Protein Structure Initiative Structures of the Month.

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.

Cell mopping up.

This image mostly shows normal cultured epithelial cells expressing green fluorescent protein targeted to the Golgi apparatus (yellow-green) and stained for actin (magenta) and DNA (cyan). The middle cell is an abnormal large multinucleated cell. All the cells in this image have a Golgi but not all are expressing the targeted recombinant fluorescent protein.