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).

Ionic and covalent bonds hold molecules, like sodium chloride and chlorine gas, together. Hydrogen bonds among molecules, notably involving water, also play an important role in biology. See image 2519 for an unlabeled version of this illustration. Featured in The Chemistry of Health.

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.

Sepsis is the body’s overactive and extreme response to an infection. More than 1.7 million people get sepsis each year in the United States. Without prompt treatment, sepsis can lead to tissue damage, organ failure, and death. Many NIGMS-supported researchers are working to improve sepsis diagnosis and treatment. Learn more with our sepsis featured topic page.

See 6551 for the Spanish version of this infographic.

CCD-1 is an enzyme produced by the bacterium Clostridioides difficile that helps it resist antibiotics. Using X-ray crystallography, researchers determined the structure of a CCD-1 molecule and a molecule of the antibiotic cefotaxime bound together. The structure revealed that CCD-1 provides extensive hydrogen bonding and stabilization of the antibiotic in the active site, leading to efficient degradation of the antibiotic.

Related to images 6764, 6765, and 6767.

X-ray co-crystal structure of Src kinase bound to a DNA-templated macrocycle inhibitor. Related to images 3413, 3414, 3415, 3416, 3417, and 3418.

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.

Mitochondria are the powerhouses of the cells, generating the energy the cells need to do their tasks and to stay alive. Researchers have studied mitochondria for some time because when these cell organelles don't work as well as they should, several diseases develop. In this photograph of cow cells taken with a microscope, the mitochondria were stained in bright yellow to visualize them in the cell. The large blue dots are the cell nuclei and the gray web is the cytoskeleton of the cells.

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.

An adult Hawaiian bobtail squid, Euprymna scolopes, (~4 cm) surrounded by newly hatched juveniles (~2 mm) in a bowl of seawater.

Related to image 7011 and video 7012.

A drug's life in the body. Medicines taken by mouth pass through the liver before they are absorbed into the bloodstream. Other forms of drug administration bypass the liver, entering the blood directly. See 2528 for a labeled version of this illustration. Featured in Medicines By Design.

Learn about how bacteria and viruses differ, how they each can make you sick, and how they can or cannot be treated. Discover more resources from NIGMS’ Pathways collaboration with Scholastic. View the video on YouTube for closed captioning.

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), Arp2 (green), and DAPI to visualize the nucleus (blue). Arp2, a subunit of the Arp2/3 complex, is localized at the lamellipodia leading edge of ARPC3+/+ fibroblast cells. Related to images 3329, 3330, 3331, 3332, and 3333.

This video shows an instance of abnormal mitosis where chromosomes are late to align. The video demonstrates the spindle checkpoint in action: just one unaligned chromosome can delay anaphase and the completion of mitosis. The cells shown are S3 tissue cultured cells from Xenopus laevis, African clawed frog.

The world's smallest motor, ATP synthase, generates energy for the cell. See image 2518 for a labeled version of this illustration. Featured in The Chemistry of Health.

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.

Related to images 1010, 1011, 1012, 1013, 1015, 1016, 1017, 1018, 1019, and 1021.

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.

This fruit fly expresses green fluorescent protein (GFP) in the same pattern as the period gene, a gene that regulates circadian rhythm and is expressed in all sensory neurons on the surface of the fly.

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.

HIV is a retrovirus, a type of virus that carries its genetic material not as DNA but as RNA. Long before anyone had heard of HIV, researchers in labs all over the world studied retroviruses, tracing out their life cycle and identifying the key proteins the viruses use to infect cells. When HIV was identified as a retrovirus, these studies gave AIDS researchers an immediate jump-start. The previously identified viral proteins became initial drug targets. See images 2513 and 2515 for other versions of this illustration. Featured in The Structures of Life.

A study published in March 2012 used cryo-electron microscopy to determine the structure of the DNA replication origin recognition complex (ORC), a semi-circular, protein complex (yellow) that recognizes and binds DNA to start the replication process. The ORC appears to wrap around and bend approximately 70 base pairs of double stranded DNA (red and blue). Also shown is the protein Cdc6 (green), which is also involved in the initiation of DNA replication. The video shows the structure from different angles. See related image 3597.

Proteins in the neural tissues of this zebrafish embryo direct cells to line up and form the neural tube, which will become the spinal cord and brain. Studies of zebrafish embryonic development may help pinpoint the underlying cause of common neural tube defects--such as spina bifida--which occur in about 1 in 1,000 newborn children.

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

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.

This microscopic image shows a chromatin fiber--a DNA molecule bound to naturally occurring proteins.

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 3493.

In this image, viewed with a ZEISS ORION NanoFab microscope, the community of cells lining a mouse airway is magnified more than 10,000 times. This collection of cells, known as the mucociliary escalator, is also found in humans. It is our first line of defense against inhaled bacteria, allergens, pollutants, and debris. Malfunctions in the system can cause or aggravate lung infections and conditions such as asthma and chronic obstructive pulmonary disease. The cells shown in gray secrete mucus, which traps inhaled particles. The colored cells sweep the mucus layer out of the lungs.

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

Enzymes convert substrates into products very quickly. See image 2522 for a labeled version of this illustration. Featured in The Chemistry of Health.

Cell showing overproduction of the ARTS protein (red). ARTS triggers apoptosis, as shown by the activation of caspase-3 (green) a key tool in the cell's destruction. The nucleus is shown in blue. Image is featured in October 2015 Biomedical Beat blog post Cool Images: A Halloween-Inspired Cell Collection.

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 TRPA1 protein is responsible for the burn you feel when you taste a bite of sushi topped with wasabi. Known therefore informally as the "wasabi receptor," this protein forms pores in the membranes of nerve cells that sense tastes or odors. Pungent chemicals like wasabi or mustard oil cause the pores to open, which then triggers a tingling or burn on our tongue. This receptor also produces feelings of pain in response to chemicals produced within our own bodies when our tissues are damaged or inflamed. Researchers used cryo-EM to reveal the structure of the wasabi receptor at a resolution of about 4 angstroms (a credit card is about 8 million angstroms thick). This detailed structure can help scientists understand both how we feel pain and how we can limit it by developing therapies to block the receptor. For more on cryo-EM see the blog post Cryo-Electron Microscopy Reveals Molecules in Ever Greater Detail.

Featured in the March 15, 2012 issue of Biomedical Beat. Related to Hsp33 Figure 1, image 3354.

A computer model of the cell membrane, where the plasma membrane is red, endoplasmic reticulum is yellow, and mitochondria are blue. This image relates to a July 27, 2009 article in Computing Life.

Fruit fly (Drosophila melanogaster) ovaries with DNA shown in magenta and actin filaments shown in light blue. This image was captured using a confocal laser scanning microscope.

Related to image 6806.

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

Reactivating telomerase in our cells does not appear to be a good way to extend the human lifespan. Cancer cells reactivate telomerase.

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.

Multiple anthrax bacteria (green) being enveloped by an immune system cell (purple). Anthrax bacteria live in soil and form dormant spores that can survive for decades. When animals eat or inhale these spores, the bacteria activate and rapidly increase in number. Today, a highly effective and widely used vaccine has made the disease uncommon in domesticated animals and rare in humans.

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