Sylvain Engilberge

Sample-efficient time-resolved X-ray crystallography with serial small wedges

This paper introduces a method to efficiently capture time-resolved structural changes in proteins using small crystal rotations and merging diffraction images across crystals.

Time-resolved functional rotation crystallography probes protein dynamics during enzymatic catalysis

This paper introduces TR-FRX, a method to study protein dynamics during enzymatic catalysis using time-resolved crystallography, and applies it to lysozyme and malate dehydrogenase.

Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes

The paper compares aromatic ring flip kinetics in GB1 protein across crystals, IgG complexes, and solution, showing reduced flipping in crystals and revealing how crystal environments restrain motion.

Integrated structural dynamics uncover new modes of B12 photoreceptor activation

The paper describes the photoactivation mechanism of the B12 photoreceptor CarH using structural and spectroscopic methods, revealing unique intermediates that drive tetramer dissociation.

Atomic resolution structures of the methane-activating enzyme in anaerobic methanotrophy reveal extensive post-translational modifications.

The paper determines atomic structures of MCRs from anaerobic methanotrophic archaea, revealing conserved structures and post-translational modifications.

Mini-bacterioferritins: Structural insight into a new type of ferritin-like protein from an anaerobic methane-oxidising archaeon

The paper identifies and characterizes mini-bacterioferritin, a novel ferritin-like protein from an anaerobic methane-oxidizing archaeon, revealing its structure and evolutionary relationships.

De novo determination of mosquitocidal Cry11Aa and Cry11Ba structures from naturally-occurring nanocrystals

The paper determines the structures of Cry11Aa and Cry11Ba toxins using serial femtosecond crystallography, revealing new insights into their in vivo crystallization patterns and toxicity.

Chimeric single α-helical domains as rigid fusion protein connections for protein nanotechnology and structural biology

The paper demonstrates that the ER/K motif (SAH) can rigidly connect protein domains, enabling the formation of ordered crystals and new applications in protein nanotechnology.