Both instruments shown were developed by CellFree Sciences of Yokohama, Japan. The instrument on the left, the GeneDecoder 1000, can generate 384 proteins from their corresponding genes, or gene fragments, overnight. It is used to screen for properties such as level of protein production and degree of solubility. The instrument on the right, the Protemist Protein Synthesizer, is used to generate the larger amounts of protein needed for protein structure determinations.

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 version of this illustration that isn't numbered and 2547 for a an entirely unlabeled version. Featured in The New Genetics.

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 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.

Acetylsalicylate (bottom) is the aspirin of today. Adding a chemical tag called an acetyl group (shaded box, bottom) to a molecule derived from willow bark (salicylate, top) makes the molecule less acidic (and easier on the lining of the digestive tract), but still effective at relieving pain. See image 2529 for an unlabeled version of this illustration. Featured in Medicines By Design.

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.

This 2-hour-old fly embryo already has a blueprint for its formation, and the process for following it is so precise that the difference of just a few key molecules can change the plans. Here, blue marks a high concentration of Bicoid, a key signaling protein that directs the formation of the fly's head. It also regulates another important protein, Hunchback (green), that further maps the head and thorax structures and partitions the embryo in half (red is DNA). The yellow dots overlaying the embryo plot the concentration of Bicoid versus Hunchback proteins within each nucleus. The image illustrates the precision with which an embryo interprets and locates its halfway boundary, approaching limits set by simple physical principles. This image was a finalist in the 2008 Drosophila Image Award.

By mixing fluorescent dyes like an artist mixes paints, scientists are able to color code individual chromosomes. The technique, abbreviated multicolor-FISH, allows researchers to visualize genetic abnormalities often linked to disease. In this image, "painted" chromosomes from a person with a hereditary disease called Werner Syndrome show where a piece of one chromosome has fused to another (see the gold-tipped maroon chromosome in the center). As reported by molecular biologist Jan Karlseder of the Salk Institute for Biological Studies, such damage is typical among people with this rare syndrome.

This image shows an osteosarcoma cell with DNA in blue, energy factories (mitochondria) in yellow, and actin filaments—part of the cellular skeleton—in purple. One of the few cancers that originate in the bones, osteosarcoma is rare, with about a thousand new cases diagnosed each year in the United States.

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

Many of today's medicines come from products found in nature, such as this sponge found off the coast of Palau in the Pacific Ocean. Chemists have synthesized a compound called Palau'amine, which appears to act against cancer, bacteria and fungi. In doing so, they invented a new chemical technique that will empower the synthesis of other challenging molecules.

Enzymes convert substrates into products very quickly. See image 2521 for an unlabeled version of this illustration. Featured in The Chemistry of Health.

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.

This normal human skin cell was treated with a growth factor that triggered the formation of specialized protein structures that enable the cell to move. We depend on cell movement for such basic functions as wound healing and launching an immune response.

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

At the root tips of the mustard plant Arabidopsis thaliana (red), two proteins work together to control the uptake of water and nutrients. When the cell division-promoting protein called Short-root moves from the center of the tip outward, it triggers the production of another protein (green) that confines Short-root to the nutrient-filtering endodermis. The mechanism sheds light on how genes and proteins interact in a model organism and also could inform the engineering of plants.

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.

Two highly stressed osteosarcoma cells are shown with a set of green droplet-like structures followed by a second set of magenta droplets. These droplets are composed of fluorescently labeled stress-response proteins, either G3BP or UBQLN2 (Ubiquilin-2). Each protein is undergoing a fascinating process, called phase separation, in which a non-membrane bound compartment of the cytoplasm emerges with a distinct environment from the surrounding cytoplasm. Subsequently, the proteins fuse with like proteins to form larger droplets, in much the same way that raindrops merge on a car’s windshield.

Real-time movie of young squids. Squids are often used as research organisms due to having the largest nervous system of any invertebrate, complex behaviors like instantaneous camouflage, and other unique traits.

This video was taken with polychromatic polarization microscope, as described in the Scientific Reports paper “Polychromatic Polarization Microscope: Bringing Colors to a Colorless World” by Shribak. The color is generated by interaction of white polarized light with the squid’s transparent soft tissue. The tissue works as a living tunable spectral filter, and the transmission band depends on the molecular orientation. When the young squid is moving, the tissue orientation changes, and its color shifts accordingly.

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 difference in how the proteins in each compartment mix with water and with each other. These differences let them 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 3791, image 3792 and image 3793.

A three-dimensional representation of the structure of E2, a key antigen protein involved with hepatitis C virus infection.

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.

These images show frog cells in interphase. The cells are Xenopus XL177 cells, which are derived from tadpole epithelial cells. The microtubules are green and the chromosomes are blue. Related to 3442.

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.

Molecular model of the struture of heme. Heme is a small, flat molecule with an iron ion (dark red) at its center. Heme is an essential component of hemoglobin, the protein in blood that carries oxygen throughout our bodies. This image first appeared in the September 2013 issue of Findings Magazine. View side view of heme here 3539.

Histone proteins loop together with double-stranded DNA to form a structure that resembles beads on a string. See image 2560 for an unlabeled version of this illustration. Featured in The New Genetics.

Drosophila adult brain showing that an adipokine (fat hormone) generates a response from neurons (aqua) and regulates insulin-producing neurons (red).

Related to images 6982, 6983, and 6984.

Early on, this Arabidopsis plant embryo picks sides: While one end will form the shoot, the other will take root underground. Short pieces of RNA in the bottom half (blue) make sure that shoot-forming genes are expressed only in the embryo's top half (green), eventually allowing a seedling to emerge with stems and leaves. Like animals, plants follow a carefully orchestrated polarization plan and errors can lead to major developmental defects, such as shoots above and below ground. Because the complex gene networks that coordinate this development in plants and animals share important similarities, studying polarity in Arabidopsis--a model organism--could also help us better understand human development.

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.

This image shows neonatal mouse heart cells. These cells were grown in the lab on a chip that aligns the cells in a way that mimics what is normally seen in the body. Green shows the protein N-cadherin, which indicates normal connections between cells. Red indicates the muscle protein actin, and blue indicates the cell nuclei. The work shown here was part of a study attempting to grow heart tissue in the lab to repair damage after a heart attack. Image and caption information courtesy of the California Institute for Regenerative Medicine. Related to images 3281 and 3283.

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.

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).

Detailed three-dimensional reconstruction of a tubular matrix in a thin section of the peripheral endoplasmic reticulum between the plasma membranes of the cell.
The endoplasmic reticulum (ER) is a continuous membrane that extends like a net from the envelope of the nucleus outward to the cell membrane. The ER plays several roles within the cell, such as in protein and lipid synthesis and transport of materials between organelles.
Shown here is a three-dimensional representation of the peripheral ER microtubules. Related to images 5855 and 5856

This ribbon drawing of a protein hand drawn and colored by researcher Jane Richardson in 1981 helped originate the ribbon representation of proteins that is now ubiquitous in molecular graphics. The drawing shows the 3-dimensional structure of the protein triose phosphate isomerase. The green arrows represent the barrel of eight beta strands in this structure and the brown spirals show the protein's eight alpha helices. A black and white version of this drawing originally illustrated a review article in Advances in Protein Chemistry, volume 34, titled "Anatomy and Taxonomy of Protein Structures." The illustration was selected as Picture of The Day on the English Wikipedia for November 19, 2009. Other important and beautiful images of protein structures by Jane Richardson are available in her Wikimedia gallery.

This image shows the hierarchical ontology of genes, cellular components and processes derived from large genomic datasets. From Dutkowski et al. A gene ontology inferred from molecular networks Nat Biotechnol. 2013 Jan;31(1):38-45. Related to 3437.

Three-dimensional reconstruction of a tubular matrix in a thin section of the peripheral endoplasmic reticulum between the plasma membranes of the cell.
The endoplasmic reticulum (ER) is a continuous membrane that extends like a net from the envelope of the nucleus outward to the cell membrane. The ER plays several roles within the cell, such as in protein and lipid synthesis and transport of materials between organelles.
Shown here are super-resolution microscopic images of the peripheral ER showing the structure of an ER tubular matrix between the plasma membranes of the cell. See image 5857 for a more detailed view of the area outlined in white in this image. For another view of the ER tubular matrix see image 5855

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 2453.

These smooth muscle cells were derived from human embryonic stem cells. The nuclei are stained blue, and the proteins of the cytoskeleton are stained green. Image and caption information courtesy of the California Institute for Regenerative Medicine.

A model of the molecule himastatin overlaid on an image of Bacillus subtilis bacteria. Scientists first isolated himastatin from the bacterium Streptomyces himastatinicus, and the molecule shows antibiotic activity. The researchers who created this image developed a new, more concise way to synthesize himastatin so it can be studied more easily. They also tested the effects of himastatin and derivatives of the molecule on B. subtilis.

More information about the research that produced this image can be found in the Science paper “Total synthesis of himastatin” by D’Angelo et al.

Related to image 6848 and video 6851.

A global "map of the protein structure universe." The Berkeley Structural Genomics Center has developed a method to visualize the vast universe of protein structures in which proteins of similar structure are located close together and those of different structures far away in the space. This map, constructed using about 500 of the most common protein folds, reveals a highly non-uniform distribution, and shows segregation between four elongated regions corresponding to four different protein classes (shown in four different colors). Such a representation reveals a high-level of organization of the protein structure universe.

This fluorescent microscope image shows human embryonic stem cells whose nuclei are stained green. Blue staining shows the surrounding supportive feeder cells. Image and caption information courtesy of the California Institute for Regenerative Medicine. See related image 3275.

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

Related to image 5871.

Staphylococcus aureus bacteria (blue) on the porous coating of a femoral hip stem used in hip replacement surgery. The relatively rough surface of an implant is a favorable environment for bacteria to attach and grow. This can lead to the development of biofilms, which can cause infections. The researchers who took this image are working to understand where biofilms are likely to develop. This knowledge could support the prevention and treatment of infections. A scanning electron microscope was used to capture this image.

More information on the research that produced this image can be found in the Antibiotics paper "Free-floating aggregate and single-cell-initiated biofilms of Staphylococcus aureus" by Gupta et al.

Related to image 6803 and video 6805.

A light organ (~0.5 mm across) of a Hawaiian bobtail squid, Euprymna scolopes, stained blue. At the time of this image, the crypts within the tissues of only one side of the organ had been colonized by green-fluorescent protein-labeled Vibrio fischeri cells, which can be seen here in green. This image was taken using confocal fluorescence microscopy.

Related to images 7016, 7017, 7018, and 7019.

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.

These neurons are derived from mouse embryonic stem cells. Red shows cells making a protein called TH that is characteristic of the neurons that degenerate in Parkinson's disease. Green indicates a protein that's found in all neurons. Blue indicates the nuclei of all cells. Studying dopaminergic neurons can help researchers understand the origins of Parkinson's disease and could be used to screen potential new drugs. Image and caption information courtesy of the California Institute for Regenerative Medicine. Related to images 3270 and 3285.

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.

These mitochondria (red) are from the heart muscle cell of a rat. Mitochondria have an inner membrane that folds in many places (and that appears here as striations). This folding vastly increases the surface area for energy production. Nearly all our cells have mitochondria. Related to image 3664.

Map of microtubule growth rates. Rates are color coded. This is an example of NIH-supported research on single-cell analysis. Related to 2798 , 2799, 2801, 2802 and 2803.

Cilia (cilium in singular) are complex molecular machines found on many of our cells. One component of cilia is the doublet microtubule, a major part of cilia’s skeletons that give them support and shape. This animated image is a partial model of a doublet microtubule’s structure based on cryo-electron microscopy images. Video can be found here 6549.

High-resolution time lapse of epithelial (skin) cell migration and wound healing. It shows an image taken every 13 seconds over the course of almost 14 minutes. The images were captured with quantitative orientation-independent differential interference contrast (DIC) microscope (left) and a conventional DIC microscope (right).

More information about the research that produced this video 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.