The structure of the catalytic chain of Methanococcus jannaschii aspartate transcarbamoylase has been determined in a hexagonal crystal form and gives insight into the possible paths that the substrate carbamoyl phosphate may follow to reach the active site during catalysis.
A trypsin-resistant catalytic domain of human calcineurin α (A subunit, residues 20–347) was crystallized in space group P21212. An X-ray diffraction data set was collected to 2.87 Å resolution and the structure was solved by molecular replacement.
Crystals of hydroquinone dioxygenase from Sphingomonas sp. strain TTNP3 belonged to space group P21 and contained two heterotetramers in the asymmetric unit related by 222 noncrystallographic symmetry. X-ray data were collected to a maximum resolution of 2.5 Å using a synchrotron source.
The crystallization and preliminary X-ray diffraction analysis of a novel chloromuconolactone dehalogenase from R. opacus 1CP are described. The oligomeric state was determined based on the self-rotation function.
The utility of differential scanning fluorimetry for homogeneity assessment and crystallization improvement of PLP-dependent enzymes is demonstrated using the potential drug target BioA from M. tuberculosis.
An on-column ligand- and detergent-exchange method was developed to obtain ligand–protein complexes for an adamantane series of compounds with 11β-HSD1 after a variety of other complexation methods had failed. An interesting byproduct of the method was the observation of artificial trimers in the crystal structures.