Open AccessCrystallization and preliminary X‐ray analysis of the complex of NADH and 3α‐hydroxysteroid dehydrogenase from Pseudomonas sp. B‐0831
Author(s) -
Kataoka Sachiyo,
Nakamura Shota,
Ohkubo Tadayasu,
Ueda Shigeru,
Uchiyama Susumu,
Kobayashi Yuji,
Oda Masayuki
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106016861
Subject(s) - orthorhombic crystal system , crystallization , dehydrogenase , dimer , nad+ kinase , chemistry , crystallography , molecule , epimer , stereochemistry , resolution (logic) , enzyme , biochemistry , crystal structure , organic chemistry , artificial intelligence , computer science
The NAD(P) + ‐dependent enzyme 3α‐hydroxysteroid dehydrogenase (3α‐HSD) catalyzes the reversible interconversion of hydroxyl and oxo groups at position 3 of the steroid nucleus. The complex of NADH and 3α‐HSD from Pseudomonas sp. B‐0831 was crystallized by the hanging‐drop vapour‐diffusion method. Refinement of crystallization conditions with microseeding improved the quality of the X‐ray diffraction data to a resolution of 1.8 Å. The crystals belonged to the orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 62.46, b = 82.25, c = 86.57 Å, and contained two molecules, reflecting dimer formation of 3α‐HSD, in the asymmetric unit.