The crystal structure of Aquifex aeolicus TrmH, a member of the a/b-knot superfamily responsible for O methylation of G18 of tRNAs, was determined to 1.85 Å resolution using the molecular-replacement method.
Cloning, purification and crystallization of T. thermophilus proline dehydrogenase is reported. The detergent n-octyl β-D-glucopyranoside was used to reduce polydispersity, which enabled crystallization.
Crystals of pseudechetoxin and pseudecin, potent peptidic inhibitors of cyclic nucleotide-gated ion channels, have been prepared and X-ray diffraction data have been collected to 2.25 and 1.90 Å resolution, respectively.
This report describes the crystallization of a recombinant flavoprotein amine dehydrogenase/oxidase with specificity for L-proline from the hyperthermophile P. furiosus DSM 3638 and X-ray diffraction data collection. Crystals belonged to space group P1 and diffracted to a resolution of 3.3 Å.
This report describes the crystallization and X-ray diffraction data collection of three types (wild-type, W416F/V435W and C9S/C268S) of B. stearothermophilus. Crystals of C9S/C268S belonged to space group P6222 and diffracted to a resolution of 2.4 Å.
Crystals of the complex formed between the bacterial membrane protein OmpC and the antibacterial protein lactoferrin suitable for high-resolution structure determination have been obtained. The crystals belong to the hexagonal space group P6, with unit-cell parameters a = b = 116.3, c = 152.4 Å.
M. tuberculosis diaminopimelate decarboxylase, the enzyme that catalyzes the final step of lysine biosynthesis, has been cloned, expressed, purified and crystallized in the absence of cofactor or substrate.
A thaumatin-like antifungal protein, NP24-I, has been isolated from ripe tomato fruits. It was crystallized by the vapour-diffusion method and data were collected to 2.45 Å. The structure was solved by molecular replacement.