Full-matrix least squares is taken as the basis for an examination of protein structure
precision. A two-atom protein model is used to compare the precisions of unrestrained and …

Abstract Structure‐based design usually focuses upon the optimization of ligand affinity.
However, successful drug design also requires the optimization of many other properties …

The fundamental importance of water molecules at drug–protein interfaces is now widely
recognised and a significant feature in structure-based drug design. Experimental methods …

A database has been compiled documenting the peptide conformations and geometries
from 70 diverse proteins refined at 1.75 Å or better. Analysis of the well‐ordered residues …

Peroxidases, oxygenases and catalases have similar high-valent metal-ion intermediates in
their respective reaction cycles. In this review, haem-based examples will be discussed. The …

Water often plays a key role in protein structure, molecular recognition, and mediating
protein–ligand interactions. Thus, free energy calculations must adequately sample water …

Flash-freezing, which has become routine in macromolecular X-ray crystallography, causes
the crystal to contract substantially. In the case of Escherichia coli β-galactosidase the …

We have re-refined the X-ray structure of the heme site in cytochrome c 553, supplementing
the crystallographic data with quantum chemical geometry optimizations, instead of the …

The hydration structure of bovine β-trypsin was investigated in cryogenic X-ray diffraction
experiments. Three crystal forms of the enzyme inhibited by benzamidine with different …

In 1970, at a time when structural information of one atom was stored on a single punched
card, the crystallographers Helen M. Berman, Edgar Meyer, and Gerson Cohen began …