The following articles are a selection of those recently accepted for publication in Acta Crystallographica Section F: Structural Biology Communications.
Development of a high-throughput crystal structure-determination platform for JAK1 using a novel metal-chelator soaking system
Active JAK1 kinase domain was crystallized with MgADP and soaked in the presence of EDTA to allow displacement of the nucleotide by compounds of interest. This high-throughput method of structure determination may be widely applicable to other protein kinases and small-molecule ATP-competitive ligands.
The structure of the metallo-β-lactamase VIM-2 in complex with a triazolylthioacetamide inhibitor
The crystal structure of a triazolylthioacetamide inhibitor in complex with Verona integron-encoded metallo-β-lactamase 2 (VIM-2) is reported at a resolution of 1.50 Å. The structure shows that the inhibitor binds to the active site of the enzyme and reveals detailed information on the inhibitor interactions.
Natural and non-natural amino-acid side-chain substitutions: affinity and diffraction studies of meditope–Fab complexes
The structure–affinity relationship of meditope–cetuximab complexes is investigated by measuring their affinity using surface plasmon resonance and determining their structures using X-ray crystallography.
Crystal structure of a phosphoribosyl anthranilate isomerase from the hyperthermophilic archaeon Thermococcus kodakaraensis
The crystal structure of a phosphoribosyl anthranilate isomerase from the hyperthermophilic archaeon T. kodakaraensis was determined in space groups P1 and C2 at 1.75 and 1.85 Å resolution, respectively.
Crystal structures of a yeast 14-3-3 protein from Lachancea thermotolerans in the unliganded form and bound to a human lipid kinase PI4KB-derived peptide reveal high evolutionary conservation
Crystal structures of a 14-3-3 protein (Bmh1) from the yeast L. thermotolerans in the unliganded form and in complex with a peptide from a human homologue (PI4KB) of its binding partner Pik1 reveal the high evolutionary conservation of 14-3-3 proteins. Indeed, the yeast 14-3-3 protein binds its human-derived ligand in a manner highly similar to that of human 14-3-3 proteins.