Crystallization and preliminary X-ray diffraction analysis of the organophosphorus hydrolase OPHC2 from Pseudomonas pseudoalcaligenes

An organophosphorus hydrolase from P. pseudoalcaligenes named OPHC2 has been crystallized. Combined with biochemical characterization, it is expected that the structure of this protein will provide insight into the catalytic mechanism of organophosphorus hydrolysis and will highlight the role of key residues involved in substrate specificity.

Crystallization and preliminary X-ray diffraction analysis of a DING protein from Pseudomonas aeruginosa PA14

A DING protein from P. aeruginosa strain PA14, named PA14DING or LapC, has been crystallized. The crystals belonged to the monoclinic space group P2₁ and diffracted to 1.9 Å resolution.

Crystallization and preliminary X-ray diffraction analysis of a high-affinity phosphate-binding protein endowed with phosphatase activity from Pseudomonas aeruginosa PAO1

A phosphate-binding protein endowed with phosphatase activity, previously dubbed LapA, from P. aeruginosa PAO1 has been crystallized. The crystals diffracted to 0.87 Å resolution and belonged to space group P2₁.

Crystallization and preliminary X-ray diffraction analysis of the lactonase VmoLac from Vulcanisaeta moutnovskia

A phosphotriesterase-like lactonase dubbed VmoLac isolated from the hyperthermophilic crenarchaeon V. moutnovskia was purified and crystallized. A diffraction data set was collected to 2.4 Å resolution.