Paul Langan

TL;DR: Comparison of X-ray structures of several ternary substrate and product complexes of the catalytic subunit of cAMP-dependent protein kinase (PKAc) with different bound metal ions reveals conformational, coordination, and hydrogen bonding changes that might occur during the reaction and shed new light on its mechanism, roles of metals, and active site residues.

TL;DR: The ternary model, refined to 2.3 A resolution, provides an accurate template for testing the feasibility of identifying dual-site inhibitors, compounds that target both the substrate and cofactor-binding site, and two structurally distinct compounds were verified that inhibit baDHFR at low microM concentrations.

TL;DR: It is demonstrated, for the first time, that neural networks can learn peak shapes and be used to integrate Bragg peaks, and it is expected that integration using neural Networks can be further developed to increase the quality of neutron, electron and X-ray crystallography data.

TL;DR: The Protein Crystallography Station (PCS) as mentioned in this paper was built and tested at the Los Alamos Neutron Science Center (LASC) for protein diffraction.

TL;DR: X-ray and neutron crystallographic studies are presented to locate H and D atoms during the respective isomerization and epimerization of L-arabinose to L- ribulose and L-ribose, respectively and it is proposed that these complexes containing Ni(2+) cofactors are Michaelis-like and the isomersization between these two sugars proceeds via a cis-ene-diol mechanism.