A simple technique to classify diffraction data from dynamic proteins according to individual polymorphs

The dynamics of proteins can be explored from polymorphs observed by the clustering of multiple data wedges.

Highlighting the factors governing transglycosylation in the GH5_5 endo-1,4-β-glucanase RBcel1

An enzymatic and structural study identifying the factors influencing the transglycosylase activity of RBcel1, a member of glycoside hydrolase family 5, is reported.

High-resolution structures of the bound effectors avadomide (CC-122) and iberdomide (CC-220) highlight advantages and limitations of the MsCI4 soaking system

Using the MsCI4 soaking system, the binding of the next-generation thalidomide-derived immunomodulatory drugs avadomide (CC-122) and iberdomide (CC-220) to cereblon was characterized at high resolution, highlighting the utility of the MsCI4 system for studies of the structure–activity relationship of cereblon effectors.

The parallel-stranded d(CGA) duplex is a highly predictable structural motif with two conformationally distinct strands

The first structural characterization of long tandem repeats of the d(CGA) triplet motif in the parallel-stranded duplex form is provided and the results show that each strand within the duplex is conformationally distinct and plays a unique role in accommodating duplex asymmetry. The structural uniformity of tandem d(CGA) base-paired triplets obtained from different solution environments further demonstrates that the d(CGA)-based parallel-stranded duplex is a robust and highly predictable structure with applications in DNA nanotechnology.

A recurring packing contact in crystals of InlB pinpoints functional binding sites in the internalin domain and the B repeat

InlB, an invasion protein from the facultative intracellular pathogen Listeria monocytogenes, is a multi-domain protein that binds and activates the human receptor tyrosine kinase MET. Three new InlB crystal structures reveal the relative orientation of the first two domains (the internalin domain and the B repeat) for the first time. A recurrent packing contact formed by all five crystallographically independent molecules highlights functionally important binding sites in the internalin domain and the B repeat.

Inhibition of Schistosoma mansoni carbonic anhydrase by the antiparasitic drug clorsulon: X-ray crystallographic and in vitro studies

The inhibitory activity of clorsulon and X-ray studies of its complexes with human carbonic anhydrase I and Schistosoma mansoni carbonic anhydrase revealed different modes of binding of this antiparasitic drug, explaining its inhibitory potency against the two enzymes.

Fast fragment- and compound-screening pipeline at the Swiss Light Source

The FFCS platform has recently been developed by the Swiss Light Source macromolecular group. It is an integrated next-generation X-ray crystallography fragment-based drug-discovery pipeline for crystal soaking, handling and data collection.

The suppressor of copper sensitivity protein C from Caulobacter crescentus is a trimeric di­sulfide isomerase that binds copper(I) with subpicomolar affinity

The characterization of the suppressor of copper sensitivity protein C from C. crescentus is reported.

Interactions between 2′-fluoro-(carbamoyl­pyridinyl)deschloroepibatidine analogues and acetylcholine-binding protein inform on potent antagonist activity against nicotinic receptors

The binding of a series of epibatidine derivatives to acetylcholine-binding protein was investigated using biolayer interferometry. The structures of three complexes inform discussion on the biological implications for interactions with nicotinic acetylcholine receptor subtypes, which are important targets for control of pain.

A new inactive conformation of SARS-CoV-2 main protease

A new inactive conformation of SARS-CoV-2 main protease that is relevant to comprehension of the catalytic cycle and for structure-based drug-design approaches is reported.

Structural basis for substrate recognition in the Phytolacca americana glycosyltransferase PaGT3

Crystal structures of the UDP glycosyltransferase PaGT3 in complex with various ligands are reported. This study sheds light on how the enzyme accommodates sugar acceptors of different shapes and sizes for successful glycosylation.

Pivotal role of a conserved histidine in Escherichia coli ribonuclease HI as proposed by X-ray crystallography

X-ray crystal structures of E. coli ribonuclease HI in complex with Mg²⁺ ions or with a Zn²⁺ ion reveal the pivotal role of a highly conserved histidine residue.