Image Credit: Kneller et al., Journal of Biological Chemistry volume 295, issue 50, P17365-17373, December 11, 2020
DOI: 10.1074/jbc.AC120.016154.
PMID: 33060199; 33453981

A recent publication in Journal of Biological Chemistry, Unusual zwitterionic catalytic site of SARS–CoV-2 main protease revealed by neutron crystallography by Danielle W. Kneller, Gwyndalyn Phillips, Kevin Weiss, Swati Pant, Qiu Zhang, Hugh M. O’Neil, Leighton Coates, and Andrey Kovalevsky described the use of crystallization and neutron crystallography to determine the neutron structure of the ligand-free SARS–CoV-2 3CL Mpro at near-physiological (room) temperature and pH and mapped the locations of hydrogen atoms (observed as deuterium) in the enzyme. Establishing the electrostatics in the enzyme active-site cavity and at the dimer interface is critical information to guide the structure-assisted and computational drug design of protease inhibitors, specifically targeting the enzyme from SARS–CoV-2. The team used Hampton Research crystallization reagents, as well as the Hampton Research Seed Bead and Siliconized 9-well glass plates and Sandwich Boxes to grow neutron-quality crystals. No nanodrops here, as 200 μl drops were used to produce the approximately 2 x 0.8 x 0.2 mm crystals.