Atomic resolution structures of the methane-activating enzyme in anaerobic methanotrophy reveal extensive post-translational modifications.

Anaerobic methanotrophic archaea (ANME) are crucial to planetary carbon cycling. They oxidise methane in anoxic niches by transferring electrons to nitrate, metal oxides, or sulfate-reducing bacteria. No ANMEs have been isolated, hampering the biochemical investigation of anaerobic methane oxidation.

Studies of the membrane-bound flavocytochrome MsrQ flavin mononucleotide (FMN)-binding site reveal an unexpected ubiquinone cofactor.

The methionine sulfoxide reductase PQ system (MsrPQ) is a newly identified type of bacterial methionine sulfoxide reductase (Msr) involved in the repair of periplasmic methionine residues that have been oxidized by hypochlorous acid. MsrP, which carries out the Msr activity, is a molybdoenzyme located in the periplasm, whereas MsrQ, an integral membrane-bound flavohemoprotein, specifically transfers electrons to MsrP to drive catalysis. MsrQ belongs to an important superfamily of heme-containing membrane-bound proteins, which includes the eukaryotic NADPH oxidases (NOX) and six-transmembrane epithelial antigen of the prostate (STEAP) ferric reductases.

An asymmetric fission island driven by shell effects in light fragments.

Nuclear fission leads to the splitting of a nucleus into two fragments. Studying the distribution of the masses and charges of the fragments is essential for establishing the fission mechanisms and refining the theoretical models. It has value for our understanding of r-process nucleosynthesis, in which the fission of nuclei with extreme neutron-to-proton ratios is pivotal for determining astrophysical abundances and understanding the origin of the elements and for energy applications.

Current and future perspectives for structural biology at the Grenoble EPN campus: a comprehensive overview.

The European Photon and Neutron campus in Grenoble is a unique site, encompassing the European Synchrotron Radiation Facility Extremely Brilliant Source, the Institut Laue-Langevin, the European Molecular Biology Laboratory and the Institut de Biologie Structurale. Here, we present an overview of the structural biology beamlines, instruments and support facilities available on the EPN campus. These include advanced macromolecular crystallography using neutrons or X-rays, small-angle X-ray or neutron scattering, cryogenic electron microscopy, and spectroscopy.

Correction: A sequential model of the contribution of preschool fluid and crystallized cognitive abilities to later school achievement.

[This corrects the article DOI: 10.1371/journal.pone.