Circadian rhythms are physical, mental, and behavioral changes that follow a 24-hour cycle. Circadian rhythms are influenced by light and regulated by the brain’s suprachiasmatic nucleus (SCN), sometimes referred to as a master clock. Learn more in NIGMS’ circadian rhythms fact sheet. See 6614 for the Spanish version of this infographic.

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, 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. 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 image 3297.

Hippocampal cells in culture with a neuron in green, showing hundreds of the small protrusions known as dendritic spines. The dendrites of other neurons are labeled in blue, and adjacent glial cells are shown in red.

This is a magnified view of an Arabidopsis thaliana leaf after several days of infection with the pathogen Hyaloperonospora arabidopsidis. The pathogen's blue hyphae grow throughout the leaf. On the leaf's edges, stalk-like structures called sporangiophores are beginning to mature and will release the pathogen's spores. Inside the leaf, the large, deep blue spots are structures called oopsorangia, also full of spores. Compare this response to that shown in Image 2781. Jeff Dangl has been funded by NIGMS to study the interactions between pathogens and hosts that allow or suppress infection.

Cryo-electron microscopy (cryo-EM) has the power to capture details of proteins and other small biological structures at the molecular level.  This image shows proteins in the capsid, or outer cover, of bacteriophage P22, a virus that infects the Salmonella bacteria. Each color shows the structure and position of an individual protein in the capsid. Thousands of cryo-EM scans capture the structure and shape of all the individual proteins in the capsid and their position relative to other proteins. A computer model combines these scans into the three-dimension image shown here. Related to image 5875.

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.

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

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) and DAPI to visualize the nucleus (blue). In the absence of functional Arp2/3 complex, ARPC3-/- fibroblast cells' leading edge morphology is significantly altered with filopodia-like structures. Related to images 3328, 3329, 3330, 3331, and 3332.

Composite image of beta-galactosidase showing how cryo-EM’s resolution has improved dramatically in recent years. Older images to the left, more recent to the right. Related to image 5882. NIH Director Francis Collins featured this on his blog on January 14, 2016.

The receptor is shown bound to an inverse agonist, ZM241385.

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.

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

A cross section of the measles virus in which six proteins work together to infect cells. The measles virus is extremely infectious; 9 out of 10 people exposed will contract the disease. Fortunately, an effective vaccine protects against infection.

For a zoomed-in look at the six important proteins, see Measles Virus Proteins.

Stereo triplet of a sea urchin embryo stained to reveal actin filaments (orange) and microtubules (blue). This image is part of a series of images: image 1048, image 1049, image 1050, image 1051 and image 1052.

A model of the molecule himastatin, which was first isolated from the bacterium Streptomyces himastatinicus. Himastatin 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.

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 6850 and video 6851.

Structural biologists create crystals of proteins, shown here, as a first step in a process called X-ray crystallography, which can reveal detailed, three-dimensional protein structures.

This Petri dish contains microscopic roundworms called Caenorhabditis elegans. Researchers used these particular worms to study how C. elegans senses the color of light in its environment.

E. coli bacteria normally live harmlessly in our intestines, but some cause disease by making toxins. One of these toxins, called Shiga toxin (green), inactivates host ribosomes (purple) by mimicking their normal binding partners, the EF-Tu elongation factor (red) complexed with Phe-tRNAPhe (orange).

Find these in the RCSB Protein Data Bank: Shiga toxin 2 (PDB entry 7U6V) and Phe-tRNA (PDB entry 1TTT).

More information about this work can be found in the J. Biol. Chem. paper "Cryo-EM structure of Shiga toxin 2 in complex with the native ribosomal P-stalk reveals residues involved in the binding interaction" by Kulczyk et. al.

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.

Various views of a mouse brain that was genetically modified so that subpopulations of its neurons glow. Researchers often study mice because they share many genes with people and can shed light on biological processes, development, and diseases in humans.

This video was captured using a light sheet microscope.

Related to images 6929 and 6930.

This video shows a controlled outbreak of transmissible avian flu among people living in Thailand. Red indicates areas of infection while blue indicates areas where a combination of control measures were implemented. The video shows how control measures contained the infection in 90 days, before it spread elsewhere.

Rhodopsin is a pigment in the rod cells of the retina (back of the eye). It is extremely light-sensitive, supporting vision in low-light conditions. Here, it is attached to arrestin, a protein that sends signals in the body. This structure was determined using an X-ray free electron laser.

This illustration shows, in simplified terms, how the CRISPR-Cas9 system can be used as a gene-editing tool. The CRISPR system has two components joined together: a finely tuned targeting device (a small strand of RNA programmed to look for a specific DNA sequence) and a strong cutting device (an enzyme called Cas9 that can cut through a double strand of DNA). This frame (4 out of 4) shows a repaired DNA strand with new genetic material that researchers can introduce, which the cell automatically incorporates into the gap when it repairs the broken DNA.

For an explanation and overview of the CRISPR-Cas9 system, see the iBiology video, and find the full CRIPSR illustration here.

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.

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.

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

3D image of Caulobacter bacterium with various components highlighted: cell membranes (red and blue), protein shell (green), protein factories known as ribosomes (yellow), and storage granules (orange).

Some children are born with a mutation in a regulatory site on this enzyme that causes them to over-secrete insulin when they consume protein. We found that a compound from green tea (shown in the stick figure and by the yellow spheres on the enzyme) is able to block this hyperactivity when given to animals with this disorder.

Cell-like compartments spontaneously emerge from scrambled frog eggs, with nuclei (blue) from frog sperm. Endoplasmic reticulum (red) and microtubules (green) are also 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: 6588, 6589, and 6590.

Georgia Tech associate professor Hang Lu holds a microfluidic chip that is part of a system that uses artificial intelligence and cutting-edge image processing to automatically examine large number of nematodes used for genetic research.

These colorful, computer-generated ribbons show the backbone of a molecule that glows a fluorescent red. The molecule, called mStrawberry, was created by chemists based on a protein found in the ruddy lips of a coral. Scientists use the synthetic molecule and other "fruity" ones like it as a dye to mark and study cell structures.

Two fruit fly (Drosophila melanogaster) egg cells, one on each side of the central black line. The colorful swirls show the circular movement of cytoplasm—called ooplasmic streaming—that occurs in late egg cell development in wild-type (right) and mutant (left) oocytes. This image was captured using confocal microscopy.

More information on the research that produced this image can be found in the Journal of Cell Biology paper “Ooplasmic flow cooperates with transport and anchorage in Drosophila oocyte posterior determination” by Lu et al.

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.

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 3375.

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.

Amid a network of blood vessels and star-shaped support cells, neurons in the brain signal each other. The mists of color show the flow of important molecules like glucose and oxygen. This image is a snapshot from a 52-second simulation created by an animation artist. Such visualizations make biological processes more accessible and easier to understand.

The green spots in this mouse brain are cells labeled with Calling Cards, a technology that records molecular events in brain cells as they mature. Understanding these processes during healthy development can guide further research into what goes wrong in cases of neuropsychiatric disorders. Also fluorescently labeled in this video are neurons (red) and nuclei (blue). Calling Cards and its application are described in the Cell paper “Self-Reporting Transposons Enable Simultaneous Readout of Gene Expression and Transcription Factor Binding in Single Cells” by Moudgil et al.; and the Proceedings of the National Academy of Sciences paper “A viral toolkit for recording transcription factor–DNA interactions in live mouse tissues” by Cammack et al. This video was created for the NIH Director’s Blog post The Amazing Brain: Tracking Molecular Events with Calling Cards.

Related to image 6780.

The "epigenetic code" controls gene activity with chemical tags that mark DNA (purple diamonds) and the "tails" of histone proteins (purple triangles). These markings help determine whether genes will be transcribed by RNA polymerase. Genes hidden from access to RNA polymerase are not expressed. See image 2563 for a labeled version of this illustration. Featured in The New Genetics.

A crawling cell with DNA shown in blue and actin filaments, which are a major component of the cytoskeleton, visible in pink. Actin filaments help enable cells to crawl. This image was captured using structured illumination microscopy.

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.

The chemical structure of the morphine molecule

Vibrio fischeri cells (~ 2 mm), labeled with green fluorescent protein (GFP), passing through a very narrow bottleneck in the tissues (red) of the Hawaiian bobtail squid, Euprymna scolopes, on the way to the crypts where the symbiont population resides. This image was taken using a confocal fluorescence microscope.

This is the first structure of a protein derived from the metagenomic sequences collected during the Sorcerer II Global Ocean Sampling project. The crystal structure shows a barrel protein with a ferredoxin-like fold and a long chain fatty acid in a deep cleft (shaded red). Featured as one of the August 2007 Protein Structure Initiative Structures of the Month.

Three-dimensional image of misfolded proteins (green) within mitochondria (red). Related to image 5878. Learn more in this press release by The American Association for the Advancement of Science.

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

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 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 3436.

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.

The white circle in this image is a Petri dish, named for its inventor, Julius Richard Petri. These dishes are one of the most common pieces of equipment in biology labs, where researchers use them to grow cells.

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.