A Janus particle being used to activate a T cell, a type of immune cell. A Janus particle is a specialized microparticle with different physical properties on its surface, and this one is coated with nickel on one hemisphere and anti-CD3 antibodies (light blue) on the other. The nickel enables the Janus particle to be moved using a magnet, and the antibodies bind to the T cell and activate it. The T cell in this video was loaded with calcium-sensitive dye to visualize calcium influx, which indicates activation. The intensity of calcium influx was color coded so that warmer color indicates higher intensity. Being able to control Janus particles with simple magnets is a step toward controlling individual cells’ activities without complex magnetic devices.

More details can be found in the Angewandte Chemie paper “Remote control of T cell activation using magnetic Janus particles” by Lee et al. This video was captured using epi-fluorescence microscopy.

Related to video 6801.

This lab space was designed for work on the induced pluripotent stem (iPS) cell collection, part of the NIGMS Human Genetic Cell Repository at the Coriell Institute for Medical Research.

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.

This pig cell is in the process of dividing. The chromosomes (purple) have already replicated and the duplicates are being pulled apart by fibers of the cell skeleton known as microtubules (green). Studies of cell division yield knowledge that is critical to advancing understanding of many human diseases, including cancer and birth defects.

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

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

This animation shows the effect of exposure to hypochlorous acid, which is found in certain types of immune cells, on bacterial proteins. The proteins unfold and stick to one another, leading to cell death.

This illustration shows, in simplified terms, how the CRISPR-Cas9 system can be used as a gene-editing tool.

Frame 1 shows the two components of the CRISPR system: a strong cutting device (an enzyme called Cas9 that can cut through a double strand of DNA), and a finely tuned targeting device (a small strand of RNA programmed to look for a specific DNA sequence).

In frame 2, the CRISPR machine locates the target DNA sequence once inserted into a cell.

In frame 3, the Cas9 enzyme cuts both strands of the DNA.

Frame 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.

Download the individual frames: Frame 1, Frame 2, Frame 3, and Frame 4.

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

The glial cells (black dots) and nerve cells (brown bands) in this developing fruit fly nerve cord formed normally despite the absence of the SPITZ protein, which blocks their impending suicide. The HID protein, which triggers suicide, is also lacking in this embryo.

A colorized scanning electron micrograph of bacteria. Scanning electron microscopes allow scientists to see the three-dimensional surface of their samples.

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

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).

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 6553 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.

Image of the colon of a mouse mono-colonized with Bacteroides fragilis (red) residing within the crypt channel. The red staining is due to an antibody to B. fragilis, the green staining is a general dye for the mouse cells (phalloidin, which stains F-actin) and the light blue glow is from a dye for visualizing the mouse cell nuclei (DAPI, which stains DNA). Bacteria from the human microbiome have evolved specific molecules to physically associate with host tissue, conferring resilience and stability during life-long colonization of the gut. Image is featured in October 2015 Biomedical Beat blog post Cool Images: A Halloween-Inspired Cell Collection.

This image shows an abnormal, tetrapolar mitosis. Chromosomes are highlighted pink. The cells shown are S3 tissue cultured cells from Xenopus laevis, African clawed frog.

The human immunodeficiency virus (HIV), shown here as tiny purple spheres, causes the disease known as AIDS (for acquired immunodeficiency syndrome). HIV can infect multiple cells in your body, including brain cells, but its main target is a cell in the immune system called the CD4 lymphocyte (also called a T-cell or CD4 cell).

Proteins are long chains of amino acids. Each protein has a unique amino acid sequence. It is still a mystery how a protein folds into the proper shape based on its sequence. Scientists hope that one day they can "watch" this folding process for any given protein. The dream has been realized, at least partially, through the use of computer simulation.

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 absent in the filopodi-like structures based leading edge of ARPC3-/- fibroblasts cells. Related to images 3328, 3330, 3331, 3332, and 3333.

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

Centrioles (green) anchor cilia (red), which project on the surface of pharynx cells of the freshwater planarian Schmidtea mediterranea. Centrioles require cellular structures called centrosomes for assembly in other animal species, but this flatworm known for its regenerative ability was unexpectedly found to lack centrosomes. From a Stowers University news release.

Xenopus laevis, the African clawed frog, has long been used as a model organism for studying embryonic development. The frog embryo on the left lacks the developmental factor Sizzled. A normal embryo is shown on the right.

C. elegans, a tiny roundworm, with a ribosomal protein glowing red and muscle fibers glowing green. Researchers used these worms to study a molecular pathway that affects aging. The ribosomal protein is involved in protein translation and may play a role in dietary restriction-induced longevity. Image created using confocal microscopy.
View group of roundworms here 6582.
View closeup of roundworms here 6583.

A colony of human embryonic stem cells (light blue) grows on fibroblasts (dark blue).

RNA interference or RNAi is a gene-silencing process in which double-stranded RNAs trigger the destruction of specific RNAs. See 2559 for a labeled version of this illustration. Featured in The New Genetics.

Individual cells are color-coded based on their identity and signaling activity using a protein circuit technology developed by the Coyle Lab. Just as a radio allows you to listen to an individual frequency, this technology allows researchers to tune into the specific “radio station” of each cell through genetically encoded proteins from a bacterial system called MinDE. The proteins generate an oscillating fluorescent signal that transmits information about cell shape, state, and identity that can be decoded using digital signal processing tools originally designed for telecommunications. The approach allows researchers to look at the dynamics of a single cell in the presence of many other cells.

Related to image 7021.

A model of thymidylate synthase complementing protein from Thermotoga maritime.

A cancer cell with three nuclei, shown in turquoise. The abnormal number of nuclei indicates that the cell failed to go through cell division, probably more than once. Mitochondria are shown in yellow, and a protein of the cell’s cytoskeleton appears in red. This video was captured using a confocal microscope.

During development, a zebrafish embryo is transformed from a ball of cells into a recognizable body plan by sweeping convergence and extension cell movements. This process is called gastrulation. Each line in this video represents the movement of a single zebrafish embryo cell over the course of 3 hours. The video was created using time-lapse confocal microscopy. Related to image 6775.

Enzymes speed up chemical reactions by reducing the amount of energy needed for the reactions. The substrate (lactose) binds to the active site of the enzyme (lactase) and is converted into products (sugars).

The three fibers of the cytoskeleton--microtubules in blue, intermediate filaments in red, and actin in green--play countless roles in the cell.

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

The proteasome is a critical multiprotein complex in the cell that breaks down and recycles proteins that have become damaged or are no longer needed. This illustration shows a protein substrate (red) that is bound through its ubiquitin chain (blue) to one of the ubiquitin receptors of the proteasome (Rpn10, yellow). The substrate's flexible engagement region gets engaged by the AAA+ motor of the proteasome (cyan), which initiates mechanical pulling, unfolding and movement of the protein into the proteasome's interior for cleavage into small shorter protein pieces called peptides. During movement of the substrate, its ubiquitin modification gets cleaved off by the deubiquitinase Rpn11 (green), which sits directly above the entrance to the AAA+ motor pore and acts as a gatekeeper to ensure efficient ubiquitin removal, a prerequisite for fast protein breakdown by the 26S proteasome. Related to video 3764.

A two-dimensional NMR spectrum of a protein, in this case a 2D 1H-15N HSQC NMR spectrum of a 228 amino acid DNA/RNA-binding protein.

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.

Yeast cells with endocytic actin patches (green). These patches help cells take in outside material. When a cell is in interphase, patches concentrate at its ends. During later stages of cell division, patches move to where the cell splits. This image was captured using wide-field microscopy with deconvolution.

Related to images 6791, 6792, 6794, 6797, 6798, and videos 6795 and 6796.

NIGMS-funded researchers led by Roger Kornberg solved the structure of RNA polymerase II. This is the enzyme in mammalian cells that catalyzes the transcription of DNA into messenger RNA, the molecule that in turn dictates the order of amino acids in proteins. For his work on the mechanisms of mammalian transcription, Kornberg received the Nobel Prize in Chemistry in 2006.

New research shows telomeres moving to the outer edge of the nucleus after cell division, suggesting these caps that protect chromosomes also may play a role in organizing DNA.

The green in this image highlights a protein called TonB, which is produced by many gram-negative bacteria, including those that cause typhoid fever, meningitis and dysentery. TonB lets bacteria take up iron from the host's body, which they need to survive. More information about the research behind this image can be found in a Biomedical Beat Blog posting from August 2013.

This map paints a colorful portrait of human genetic variation around the world. Researchers analyzed the DNA of 485 people and tinted the genetic types in different colors to produce one of the most detailed maps of its kind ever made. The map shows that genetic variation decreases with increasing distance from Africa, which supports the idea that humans originated in Africa, spread to the Middle East, then to Asia and Europe, and finally to the Americas. The data also offers a rich resource that scientists could use to pinpoint the genetic basis of diseases prevalent in diverse populations. Featured in the March 19, 2008, issue of Biomedical Beat.

A mouse's fat cells (red) are shown surrounded by a network of blood vessels (green). Fat cells store and release energy, protect organs and nerve tissues, insulate us from the cold, and help us absorb important vitamins.

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

The marine bacterium Vibrio harveyi glows when near its kind. This luminescence, which results from biochemical reactions, is part of the chemical communication used by the organisms to assess their own population size and distinguish themselves from other types of bacteria. But V. harveyi only light up when part of a large group. This communication, called quorum sensing, speaks for itself here on a lab dish, where more densely packed areas of the bacteria show up blue. Other types of bacteria use quorum sensing to release toxins, trigger disease, and evade the immune system.

These images illustrate a technique combining cryo-electron tomography and super-resolution fluorescence microscopy called correlative imaging by annotation with single molecules (CIASM). CIASM enables researchers to identify small structures and individual molecules in cells that they couldn’t using older techniques.

To become products, reactants must overcome an energy hill. See image 2525 for an unlabeled version of this illustration. Featured in The Chemistry of Health.

This illustration shows, in simplified terms, how the CRISPR-Cas9 system can be used as a gene-editing tool. This is the first frame in a series of four. 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).

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

A humorous treatment of the concept of a cycling cell.

A cell nucleus (blue) surrounded by lipid droplets (yellow). Exogenously expressed, S-tagged UBXD8 (green) recruits endogenous p97/VCP (red) to the surface of lipid droplets in oleate-treated HeLa cells. Nucleus stained with DAPI.

Those of us who get sneezy and itchy-eyed every spring or fall may have pollen grains, like those shown here, to blame. Pollen grains are the male germ cells of plants, released to fertilize the corresponding female plant parts. When they are instead inhaled into human nasal passages, they can trigger allergies.

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

Fruit flies are a common model organism for basic medical research.

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

In the top snapshots, the brain of a sleep-deprived fruit fly glows orange, marking high concentrations of a synaptic protein called Bruchpilot (BRP) involved in communication between neurons. The color particularly lights up brain areas associated with learning. By contrast, the bottom images from a well-rested fly show lower levels of the protein. These pictures illustrate the results of an April 2009 study showing that sleep reduces the protein's levels, suggesting that such "downscaling" resets the brain to normal levels of synaptic activity and makes it ready to learn after a restful night.