Diamond and graphite have a new carbon cousin called diamondiyne, with a crystal structure confirmed so far only in microscopic patches.

Abstract. Reactions of alkali-metal hexafluoridoplatinates(V), MPtF6 (M = Li, Na, K, Rb), with xenon difluoride in anhydrous hydrogen fluoride were investi

We report the crystal structure of human PITPα in complex with microcolin H at 2.0 Å resolution, revealing that microcolins bind covalently within the lipid-binding cavity and stabilize PITPα in an open conformation with a markedly enlarged cavity relative to the lipid-bound state. These results define the structural basis of PITP inhibition by microcolins and underscore the importance of using ligand-bound conformations for accurate structure-based modeling.

X-ray crystal structures of glycosyltransferase C from the Limosilactobacillus reuteri 100-23 (LrGtfC100-23) accessory secretion system were determined in its apo form and in complexes with UDP and with UDP-N-acetylglucosamine, which revealed candidate residues involved in strain-specific recognition of UDP-sugars. Site-directed mutagenesis of these residues led to a switch of the UDP-sugar binding specificities of LrGtfC100-23 and the highly homologous LrGtfC from L. reuteri ATCC 53608.

P113 is a membrane-anchored protein in Plasmodium falciparum that stabilizes the RH5 complex, facilitating erythrocyte invasion by interacting with the host receptor basigin. The helical-rich domain of P113 (residues 311–679) was crystallized, revealing a predominantly α-helical structure with two four-helix bundles and a disordered connecting region.

This study reports the co-crystallization of piperine with the peroxisome proliferator-activated receptor gamma (PPARγ) ligand-binding domain, providing detailed insights into the piperine binding position and its interactions with specific amino acids within the receptor. X-ray crystallographic analysis of the co-crystal structure revealed that piperine binds in the ligand-binding pocket of PPARγ via hydrogen-bonding and hydrophobic interactions, suggesting that it plays a role as a partial agonist or antagonist and thereby holds promise as a natural alternative to synthetic PPARγ modulators.

This communication describes the crystal structure of TRIM21 in complex with suramin, providing new opportunities to target this E3 ligase.