forthcoming articles

Abstract An automatic pipeline based on molecular replacement phases is described for the automatic crystal structure solution of proteins and DNA-RNA molecules.

The full Amber force field has been integrated into Phenix as an alternative refinement target. With a slight loss in speed, it achieves improved stereochemistry, fewer steric clashes and better hydrogen bonds.

The structural architecture of the ternary GDP–kanamycin–APH(2′′)-IIIa complex reveals no regulation of GTP hydrolysis.

Extracellular serine protease (Esp) is a glutamyl endopeptidase from S. epidermidis that plays a key role in inhibiting the growth and formation of S. aureus biofilm. This manuscript presents crystal structures of the Esp zymogen and its N-terminus locked variants, and details the role of its unusually long N-terminus in the activation and function of Esp.

Improvements to the sensitivity of the search for suitable molecular-replacement search models in SIMBAD through the use of Phaser and an ensemble-based model database are reported.

A comparison of four protein model-building pipelines (ARP/wARP, Buccaneer, Phenix AutoBuild and SHELXE) was performed using data sets from 202 experimentally phased cases, both with the data as observed and truncated to simulate lower resolutions.

High-resolution crystal structures of piperideine-6-carboxylate dehydrogenase from S. clavuligerus in its apo form and in complexes with the cofactor NAD⁺, the product α-aminoadipic acid and the substrate analogue picolinic acid are described. The data presented provide insights into ligand binding and catalysis.

A method is presented for high-speed low-volume cryo-EM specimen preparation with a device constructed from readily available components.

Crystal structures and the enzymatic properties of the GH6 Orpinomyces sp. Y102 CelC7 enzyme suggest that this enzyme may perform enzymatic hydrolysis in the same way as cellobiohydrolases and endoglucanases.