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.

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

It's probably most people's least favorite activity, but we still need to do it--take out our trash. Otherwise our homes will get cluttered and smelly, and eventually, we'll get sick. The same is true for our cells: garbage disposal is an ongoing and essential activity, and our cells have a dedicated waste-management system that helps keep them clean and neat. One major waste-removal agent in the cell is the lysosome. Lysosomes are small structures, called organelles, and help the body to dispose of proteins and other molecules that have become damaged or worn out.

This image shows a massive accumulation of lysosomes (visualized with LAMP1 immunofluorescence, in purple) within nerve cells that surround amyloid plaques (visualized with beta-amyloid immunofluorescence, in light blue) in a mouse model of Alzheimer's disease. Scientists have linked accumulation of lysosomes around amyloid plaques to impaired waste disposal in nerve cells, ultimately resulting in cell death.

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.

Model of the enzyme nicotinic acid phosphoribosyltransferase. This enzyme, from the archaebacterium, Pyrococcus furiosus, is expected to be structurally similar to a clinically important human protein called B-cell colony enhancing factor based on amino acid sequence similarities and structure prediction methods. The structure consists of identical protein subunits, each shown in a different color, arranged in a ring.

This image shows a cell in two stages of division: prometaphase (top) and metaphase (bottom). To form identical daughter cells, chromosome pairs (blue) separate via the attachment of microtubules made up of tubulin proteins (pink) to specialized structures on centromeres (green).

Related to image 5870.

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.

Microtubules in African green monkey cells. Microtubules are strong, hollow fibers that provide cells with structural support. Here, the microtubules have been color-coded based on their distance from the microscope lens: purple is closest to the lens, and yellow is farthest away. This image was captured using Stochastic Optical Reconstruction Microscopy (STORM).

Related to images 6889, 6890, and 6892.

A global "map of the protein structure universe" indicating the positions of specific proteins. The preponderance of small, less-structured proteins near the origin, with the more highly structured, large proteins towards the ends of the axes, may suggest the evolution of protein structures.

Scientists in Scotland were the first to clone an animal, this sheep named Dolly. She later gave birth to Bonnie, the lamb next to her.

PETase enzyme degrades polyester plastic (polyethylene terephthalate, or PET) into monohydroxyethyl terephthalate (MHET). Then, MHETase enzyme degrades MHET into its constituents ethylene glycol (EG) and terephthalic acid (TPA).

Find these in the RCSB Protein Data Bank: PET hydrolase (PDB entry 5XH3) and MHETase (PDB entry 6QGA).

This photo shows a Varian Unity Inova 900 MHz, 21.1 T standard bore magnet Nuclear Magnetic Resonnance (NMR) spectrometer. NMR spectroscopy provides data used to determine the structures of proteins in solution, rather than in crystal form, as in X-ray crystallography. The technique is limited to smaller proteins or protein fragments in a high throughput approach.

To splice a human gene (in this case, the one for insulin) into a plasmid, scientists take the plasmid out of an E. coli bacterium, cut the plasmid with a restriction enzyme, and splice in insulin-making human DNA. The resulting hybrid plasmid can be inserted into another E. coli bacterium, where it multiplies along with the bacterium. There, it can produce large quantities of insulin. See image 2564 for an unlabeled version of this illustration. Featured in The New Genetics.

Learn how curiosity about the world and our cells is key to scientific discoveries. Discover more resources from NIGMS’ Pathways collaboration with Scholastic. View the video on YouTube for closed captioning.

A team of chemists and physicists used nanotechnology and DNA's ability to self-assemble with matching RNA to create a new kind of chip for measuring gene activity. When RNA of a gene of interest binds to a DNA tile (gold squares), it creates a raised surface (white areas) that can be detected by a powerful microscope. This nanochip approach offers manufacturing and usage advantages over existing gene chips and is a key step toward detecting gene activity in a single cell. Featured in the February 20, 2008, issue of Biomedical Beat.

The nucleolinus is a cellular compartment that has been a lonely bystander in scientific endeavors. Although it's found in a range of species, its function has been mysterious—mainly because the structure is hard to visualize. An August 2010 study showed that the nucleolinus is crucial for cell division. When researchers zapped the structure with a laser, an egg cell didn't complete division. When the oocyte was fertilized after laser microsurgery (bottom right), the resulting zygote didn't form vital cell division structures (blue and yellow).

A computer-generated sketch of a DNA origami folded into a flower-and-bird structure. See also related image 3690.

On the left, a cross-section slice of a rat pancreas cell captured using cryo-electron tomography (cryo-ET). On the right, a 3D, color-coded version of the image highlighting cell structures. Visible features include microtubules (neon-green rods), ribosomes (small yellow circles), and vesicles (dark-blue circles). These features are surrounded by the partially visible endoplasmic reticulum (light blue). The black line at the bottom right of the left image represents 200 nm. Related to image 6607.

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, 2495, and 2488.

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.

Duplicated pair of chromosomes have exchanged material.

This illustration of an epoxide-opening cascade promoted by water emulates the proposed biosynthesis of some of the Red Tide toxins.

Model based on X-ray crystallography of the structure of a small heat shock protein complex from the bacteria, Methanococcus jannaschii. Methanococcus jannaschii is an organism that lives at near boiling temperature, and this protein complex helps it cope with the stress of high temperature. Similar complexes are produced in human cells when they are "stressed" by events such as burns, heart attacks, or strokes. The complexes help cells recover from the stressful event.

On the left, a cross-section slice of a rat pancreas cell captured using cryo-electron tomography (cryo-ET). On the right, a 3D, color-coded version of the image highlighting cell structures. Visible features include the folded sacs of the Golgi apparatus (copper), transport vesicles (medium-sized dark-blue circles), microtubules (neon green), ribosomes (small pale-yellow circles), and lysosomes (large yellowish-green circles). Black line (bottom right of the left image) represents 200 nm. This image is a still from video 6609.

Two models for how material passes through the Golgi apparatus: the vesicular shuttle model and the cisternae maturation model.

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.

2.5Å resolution reconstruction of rabbit muscle aldolase collected on a FEI/Thermo Fisher Titan Krios with energy filter and image corrector.

The body uses a variety of ion channels to transport small molecules across cell membranes.

Muscles stretch and contract when we walk, and skin splits open and knits back together when we get a paper cut. To study these contractile forces, researchers built a three-dimensional scaffold that mimics tissue in an organism. Researchers poured a mixture of cells and elastic collagen over microscopic posts in a dish. Then they studied how the cells pulled and released the posts as they formed a web of tissue. To measure forces between posts, the researchers developed a computer model. Their findings--which show that contractile forces vary throughout the tissue--could have a wide range of medical applications.

Myotonic dystrophy is thought to be caused by the binding of a protein called Mbnl1 to abnormal RNA repeats. In these two images of the same muscle precursor cell, the top image shows the location of the Mbnl1 splicing factor (green) and the bottom image shows the location of RNA repeats (red) inside the cell nucleus (blue). The white arrows point to two large foci in the cell nucleus where Mbnl1 is sequestered with RNA.

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.

Glucose (top) and sucrose (bottom) are sugars made of carbon, hydrogen, and oxygen atoms. Carbohydrates include simple sugars like these and are the main source of energy for the human body.

These cells get their name from the hairlike structures that extend from them into the fluid-filled tube of the inner ear. When sound reaches the ear, the hairs bend and the cells convert this movement into signals that are relayed to the brain. When we pump up the music in our cars or join tens of thousands of cheering fans at a football stadium, the noise can make the hairs bend so far that they actually break, resulting in long-term hearing loss.

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

Scanning electron micrograph of just-divided HeLa cells. Zeiss Merlin HR-SEM. See related images 3519, 3520, 3521, 3522.

Pigment cells are cells that give skin its color. In fishes and amphibians, like frogs and salamanders, pigment cells are responsible for the characteristic skin patterns that help these organisms to blend into their surroundings or attract mates. The pigment cells are derived from neural crest cells, which are cells originating from the neural tube in the early embryo. This image shows pigment cells from pearl danio, a relative of the popular laboratory animal zebrafish. Investigating pigment cell formation and migration in animals helps answer important fundamental questions about the factors that control pigmentation in the skin of animals, including humans. Related to images 5754, 5755, 5757 and 5758.

Planarians are freshwater flatworms that have powerful abilities to regenerate their bodies, which would seem to make them natural model organisms in which to study stem cells. But until recently, scientists had not been able to efficiently find the genes that regulate the planarian stem cell system. In this image, a single stem cell has given rise to a colony of stem cells in a planarian. Proliferating cells are red, and differentiating cells are blue. Quantitatively measuring the size and ratios of these two cell types provides a powerful framework for studying the roles of stem cell regulatory genes in planarians.

A mouse liver glows after being tagged with specially designed infrared-fluorescent protein (IFP). Since its discovery in 1962, green fluorescent protein (GFP) has become an invaluable resource in biomedical imaging. But because of its short wavelength, the light that makes GFP glow doesn't penetrate far in whole animals. So University of California, San Diego cell biologist Roger Tsien--who shared the 2008 Nobel Prize in chemistry for groundbreaking work with GFP--made infrared-fluorescent proteins (IFPs) that shine under longer-wavelength light, allowing whole-body imaging in small animals.

Human metaphase chromosomes are visible with fluorescence in vitro hybridization (FISH). Centromeric alpha satellite DNA (green) are found in the heterochromatin at each centromere. Immunofluorescence with CENP-A (red) shows the centromere-specific histone H3 variant that specifies the kinetochore.

Proteins are made of amino acids hooked end-to-end like beads on a necklace. To become active, proteins must twist and fold into their final, or "native," conformation. A protein's final shape enables it to accomplish its function. Featured in The Structures of Life.

To better understand cell movements in developing embryos, researchers isolated cells from early zebrafish embryos and grew them as clusters. Provided with the right signals, the clusters replicated some cell movements seen in intact embryos. Each line in this image depicts the movement of a single cell. The image was created using time-lapse confocal microscopy. Related to video 6776.

Serum albumin (SA) is the most abundant protein in the blood plasma of mammals. SA has a characteristic heart-shape structure and is a highly versatile protein. It helps maintain normal water levels in our tissues and carries almost half of all calcium ions in human blood. SA also transports some hormones, nutrients and metals throughout the bloodstream. Despite being very similar to our own SA, those from other animals can cause some mild allergies in people. Therefore, some scientists study SAs from humans and other mammals to learn more about what subtle structural or other differences cause immune responses in the body.

Related to entries 3725 and 3675.

T cells engulf and digest cells displaying markers (or antigens) for retroviruses, such as HIV.

X-ray co-crystal structure of Src kinase bound to a DNA-templated macrocycle inhibitor. Related to 3413, 3415, 3416, 3417, 3418, and 3419.

Structure of sortase b from the bacterium B. anthracis, which causes anthrax. Sortase b is an enzyme used to rob red blood cells of iron, which the bacteria need to survive.

Student Christina Hueneke of the Midwest Center for Structural Genomics is overseeing a protein cloning robot. The robot was designed as part of an effort to exponentially increase the output of a traditional wet lab. Part of the center's goal is to cut the average cost of analyzing a protein from $200,000 to $20,000 and to slash the average time from months to days and hours.

Multiphoton fluorescence image of HeLa cells with cytoskeletal microtubules (magenta) and DNA (cyan). Nikon RTS2000MP custom laser scanning microscope. See related images 3518, 3519, 3521, 3522.

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 2566 for an unlabeled version of this illustration. Featured in The New Genetics.

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 2571 and 2572.