The image shows the MORC2 protein frozen in ice and photographed using a special microscope that works in extreme cold called cryo-electron microscopy. This freezing technique lets us see the tiny protein's actual shape. By learning how MORC2 looks structurally, researchers can figure out what it does in our bodies and develop novel therapeutics for diseases related to MORC2.

Reference: doi.org/10.1038/s41467-025-60751-z

Heparan-alpha-glucosaminide N-acetyltransferase (HGSNAT) is a dimeric lysosomal membrane protein that catalyzes acetylation of heparan sulfate (substrate) in the lysosomal lumen. Acetyl-CoA from the cytosol acts as a co-substrate and acetyl group donor in this reaction. The artwork depicts the cryo-EM structure (EMD-41620) of the first step of the reaction, co-substrate acetyl-CoA (red) bound to HGSNAT (blue), poised to transfer the acetyl group (yellow) to the heparan sulfate in the lysosomal lumen. Acetyl-CoA on the right is faded to reflect its existence in the second active site.

Reference: doi.org/10.7554/eLife.93510.3

Captured using the L120C microscope, this delicate, flower-like structure blossomed unexpectedly in a field of negative stain. An artifact, yes—but one that mimics nature’s elegance at the nanometre scale.

Scale bar: 50 nm. (AKA: when your sample ghosts you, but art happens.)

A cat is jumping from a respiratory supercomplex inside mitochondria. This is a snapshot of a video game, currently being made, where players can navigate inside the cellular environment. Membrane geometry and large protein placement is adapted from CryoET data of mitochondria, and high resolution structures are from the PDB. 

Reference: 10.1101/2024.12.28.630444.

Life on other planets? Can we relate "planets" and "proteins?" How are they similar? The planet Mercury is made of rock and metal.

Mercury's titanium stabilizes volcanic regions, which is very beneficial because the deformation of its crust still persists. I illustrate a human actin-binding protein represented in helices and sheets. This structure is expressed in all cells of the body, especially in muscles, as it participates in muscle contraction. The gold textures are artificial visualizations of Mercury used to study the different types of metals that predominate there.. 

Reference: 10.1126/science.adg6812. PDB 8F8Q.

A structural snapshot of the muscarinic M5 receptor bound to an allosteric ligand, captured in cryogenic stillness. The receptor backbone is shown in ribbon, with side chains rendered in ball-and-stick. The allosteric ligand appears as blue spheres, locked in place, stabilising the active conformation. This image, derived from cryo-EM data, captures the moment where dynamic signalling is frozen into molecular clarity, revealing the intricate beauty of GPCR modulation at atomic resolution.

Reference:  doi: 10.1038/s41467-025-62212-z. PDB: 9EJZ

Inspired from One and Three Chairs (1965) by Joseph Kosuth, this 'art' reimagines the GLP-1 receptor in four forms: a 3D structure, its amino acid sequence, the matching nucleotide code, and a dictionary-style definition. Here, science meets conceptual art - who says receptors can't be philosophical?

This image was originally intended to be used as the cover for a journal issue. However, a professional artist was commissioned to make the cover, so my neon image was never released, until now, where I hope it has a chance to shine. It shows our proposed model for how the Bacteriophage λ proteins Redβ and λExonucelase interact together, with three monomers of each protein. Beginning as a Frankenstein’s monster of several cryo-EM and crystallography structures superimposed together, AlphaFold allowed us to expand the number of proteins and identify potential interactions, creating the complex you see here, and informing our cryo-EM data.

Reference: doi.org/10.1016/J.ENGMIC.2023.100120

Shown is the enzyme “peroxiredoxin.” This molecular hitchhiker tags along when isolating other proteins for structural determination. Cryo-EM images of these nuisance proteins can be identified and discarded. In this case, we were able to computationally purify minute amounts of peroxiredoxin and determine its structure. In the picture, five beams illuminate the complex, accenting its natural symmetry. The “stars” in the background are from shot noise during rendering, which is reminiscent of the low signal-to-noise ratio of cryo-EM and the artifactual nature of this attractive contaminant.

Cryo-EM structure of parathyroid hormone type 1 receptor (PTH1R) in complex with Gs with a ligand (shown in red).

This was my first practice using Blender, featuring EMD-8623—the first full-length active class B GPCR–G protein structure. Though its resolution may seem modest now, its impact was profound. Just like this early render, it reminds me that every journey begins with a first step—and we should never forget why we started.

Reference: doi.org/10.1038/nature22327

I study the life cycles of viruses using cryo-electron tomography, capturing them in the act of infection and host killing. When the real viruses stress me out, I crochet them instead! This cuddly virus model shows top right = the full viral villain; top left = cross-section with spikes, envelope and capsid; bottom left = the capsid; and bottom right = double-stranded RNA.

The forces of good and evil battle! A storm brews on the horizon….Will it culminate in a migraine??

I study the PAC1 receptor using cryo-EM to figure out what it looks like. Here, two models of the PAC1R show it interacting with Gs (red) and Gq (white) proteins. These are thought to exert opposing effects in the brain regarding migraine. Gs can trigger or exacerbate a migraine, whilst Gq does the opposite. Here, I’ve imagined PAC1R as playing the two roles, both little angel and devil, living on the shoulders of a migraine sufferer.