issue contents

ISSN: 2053-230X

September 2021 issue

Highlighted illustration

Cover illustration: The OXA-48-like carbapenemase OXA-436. Lund et al. [(2021), Acta Cryst. F77, 312–318] explore the reasons why the antibiotic-resistance enzyme OXA-436 has a higher enzymatic activity at physiological temperatures than its its more widespread homolog OXA-48.

research communications

link to html
Several crystal structures are analyzed of proteins that form the shells of bacterial microcompartment organelles. These new structures are from microcompartments where the metabolic substrate choline diffuses across the shell-protein pore.

link to html
The Yersinia pestis substrate-binding protein YfeA contains two polyspecific metal-binding sites, and site 2 is capable of collaborating with other protein molecules for inter-protein metal coordination. The inter-protein metal coordination can occur by multiple coordination geometries and may be flexible enough to enable metal transfer to multiple metal-binding proteins.

link to html
Protein–protein interaction between the acyltransferase VinK and the carrier protein VinL is critical for substrate transfer in vicenistatin biosynthesis. The crystal structure of the VinK–VinL covalent complex formed with a pantetheine cross-linking probe has been determined.

link to html
Possible mechanisms are demonstrated to explain why the antibiotic-resistance enzyme OXA-436 has higher catalytic rates towards last-resort antibiotics under physiological conditions compared with its more widespread homolog OXA-48.

methods communications

link to html
A novel device has been designed that could be used as both an in situ macroplate and in situ microplate for high-throughput crystal screening and in situ data collection.
Follow Acta Cryst. F
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds