Time-lapse video of yeast cells undergoing cell division. Nuclear envelopes are shown in green, and spindle pole bodies, which help pull apart copied genetic information, are shown in magenta. This video was captured using wide-field microscopy with deconvolution.

Related to images 6791, 6792, 6793, 6794, 6797, 6798, and video 6796.

The receptor is shown bound to an inverse agonist, doxepin.

Ecteinascidin 743 (ET-743, brand name Yondelis), was discovered and isolated from a sea squirt, Ecteinascidia turbinata, by NIGMS grantee Kenneth Rinehart at the University of Illinois. It was synthesized by NIGMS grantees E.J. Corey and later by Samuel Danishefsky. Multiple versions of this structure are available as entries 2790-2797.

Human embryonic stem cells differentiated into dopaminergic neurons, the type that degenerate in Parkinson's disease. Image courtesy of the California Institute for Regenerative Medicine. Related to images 3271 and 3285.

Floral pattern emerging as two bacterial species, motile Acinetobacter baylyi (red) and non-motile Escherichia coli (green), are grown together for 48 hours on 1% agar surface from a small inoculum in the center of a Petri dish.

See 6557 for a photo of this process at 24 hours on 0.75% agar surface.
See 6555 for another photo of this process at 48 hours on 1% agar surface.
See 6556 for a photo of this process at 72 hours on 0.5% agar surface.
See 6550 for a video of this process.

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.

Cell-like compartments spontaneously emerge from scrambled frog eggs. Endoplasmic reticulum (red) and microtubules (green) are visible. Video created using epifluorescence microscopy.

For more photos of cell-like compartments from frog eggs view: 6584, 6585, 6586, 6591, 6592, and 6593.

For videos of cell-like compartments from frog eggs view: 6587, 6588, and 6590.

This image shows the structure of a synapse, or junction between two nerve cells in three dimensions. From the brain of a mouse.

The fledgling field of X-ray microscopy lets researchers look inside whole cells rapidly frozen to capture their actions at that very moment. Here, a yeast cell buds before dividing into two. Colors show different parts of the cell. Seeing whole cells frozen in time will help scientists observe cells' complex structures and follow how molecules move inside them.

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.

Image of Streptococcus, a type (genus) of spherical bacteria that can colonize the throat and back of the mouth. Stroptococci often occur in pairs or in chains, as shown here.

This network map shows molecular interactions (yellow) associated with a congenital condition that causes heart arrhythmias and the targets for drugs that alter these interactions (red and blue).

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

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.

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.

The atomic structure of the morphine biosynthetic enzyme salutaridine reductase bound to the cofactor NADPH. The substrate salutaridine is shown entering the active site.

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.

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

What looks a little like distant planets with some mysterious surface features are actually assemblies of proteins normally found in the cell's nucleolus, 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 photo of nucleolus proteins in the eggs of a commonly used lab animal, the frog Xenopus laevis, shows each of the nucleolus compartments (the granular component is shown in red, the fibrillarin in yellow-green, and the fibrillar center in blue). The researchers have found that these compartments 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, video 3791 and image 3793.

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 complex between CCD-1 and the antibiotic cefotaxime (purple, yellow, and blue molecule). The structure revealed that CCD-1 provides extensive hydrogen bonding (shown as dotted lines) and stabilization of the antibiotic in the active site, leading to efficient degradation of the antibiotic.

Related to images 6764, 6765, and 6766.

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.

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.

Automated methods using micromachined silicon are used at the Northeast Collaboratory for Structural Genomics to mount protein crystals for X-ray crystallography.

During DNA replication, each strand of the original molecule acts as a template for the synthesis of a new, complementary DNA strand. See image 2543 for an unlabeled version of this illustration. Featured in The New Genetics.

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.

Multicellular yeast called snowflake yeast that researchers created through many generations of directed evolution from unicellular yeast. Cells are connected to one another by their cell walls, shown in blue. Stained cytoplasm (green) and membranes (magenta) show that the individual cells remain separate. This image was captured using spinning disk confocal microscopy.

Related to images 6969 and 6971.

Luciferase-based imaging enables visualization and quantification of internal organs and transplanted cells in live adult zebrafish. In this image, a cardiac muscle-restricted promoter drives firefly luciferase expression. This is the lateral and overhead (Bottom) view.
For imagery of the overhead view go to 3557.
For imagery of the lateral view go to 3558.
For more information about the illumated area go to 3559.

Zinc is required for the function of more than 300 enzymes, including those that help regulate gene expression, in various organisms including humans. Researchers study how plants acquire, sequester and distribute zinc to find ways to increase the zinc content of crops to improve human health. Using synchrotron X-ray fluorescence technology, they created this heat map of zinc levels in an Arabidopsis thaliana plant leaf. This image is a winner of the 2015 FASEB Bioart contest and was featured in the NIH Director's blog.

This image is a computer-generated model of the approximately 4.2 million atoms of the HIV capsid, the shell that contains the virus' genetic material. Scientists determined the exact structure of the capsid and the proteins that it's made of using a variety of imaging techniques and analyses. They then entered these data into a supercomputer that produced the atomic-level image of the capsid. This structural information could be used for developing drugs that target the capsid, possibly leading to more effective therapies. Related to image 6601.

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.

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.

Model of aspartoacylase, a human enzyme involved in brain metabolism.

The two large, central, round shapes are ovaries from a typical fruit fly (Drosophila melanogaster). The small butterfly-like structures surrounding them are fruit fly ovaries where researchers suppressed the expression of a gene that controls microtubule polymerization and is necessary for normal development. This image was captured using a confocal laser scanning microscope.

Related to image 6807.

Learn about some of the different jobs in a scientific laboratory and how researchers work as a team to make discoveries. Discover more resources from NIGMS’ Pathways collaboration with Scholastic. View the video on YouTube for closed captioning.

Featured in the March 15, 2012 issue of Biomedical Beat. Related to Hsp33 Figure 2, image 3355.

A white poppy. View cropped image of a poppy here 3423.

RNA interference or RNAi is a gene-silencing process in which double-stranded RNAs trigger the destruction of specific RNAs. See 2558 for an unlabeled version of this illustration. Featured in The New Genetics.

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

Real-time footage of Caenorhabditis elegans, a tiny roundworm, trapped by a carnivorous fungus, Arthrobotrys dactyloides. This fungus makes ring traps in response to the presence of C. elegans. When a worm enters a ring, the trap rapidly constricts so that the worm cannot move away, and the fungus then consumes the worm. The size of the imaged area is 0.7mm x 0.9mm.

This video was obtained with a polychromatic polarizing microscope (PPM) in white light that shows the polychromatic birefringent image with hue corresponding to the slow axis orientation. More information about PPM can be found in the Scientific Reports paper “Polychromatic Polarization Microscope: Bringing Colors to a Colorless World” by Shribak.

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.

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.

Model of the enzyme aminopeptidase N from the human pathogen Neisseria meningitidis, which can cause meningitis epidemics. The structure provides insight on the active site of this important molecule.

Multiple actin filaments (magenta) are organized around a dynamin helical polymer (rainbow colored) in this model derived from cryo-electron tomography. By bundling actin, dynamin increases the strength of a cell’s skeleton and plays a role in cell-cell fusion, a process involved in conception, development, and regeneration.

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.

Nerve cells have long, invisibly thin fibers that carry electrical impulses throughout the body. Some of these fibers extend about 3 feet from the spinal cord to the toes.

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).

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.

The receptor is shown bound to a partial inverse agonist, carazolol.

This is a tomographic reconstruction of a mitochondrion from an insect flight muscle. Mitochondria are cellular compartments that are best known as the powerhouses that convert energy from the food into energy that runs a range of biological processes. Nearly all our cells have mitochondria.

Cells walk along body surfaces via tiny "feet," called focal adhesions, that connect with the extracellular matrix. See image 2503 for a labeled version of this illustration.