Crystallization and preliminary X-ray diffraction analysis of mouse 3(17)alpha-hydroxysteroid dehydrogenase.
The 3(17)alpha-hydroxysteroid dehydrogenase from mouse is involved in the metabolism of oestrogens, androgens, neurosteroids and xenobiotic compounds. The enzyme was crystallized by the hanging-drop vapour-diffusion method in space group P222(1), with unit-cell parameters a = 84.91, b = 84.90, c = 95.83 A. The Matthews coefficient (VM) and the solvent content were 2.21 A3 Da(-1) and 44.6%, respectively, assuming the presence of two molecules in the asymmetric unit. Diffraction data were collected to a resolution of 1.8 A at the Swiss Light Source beamline X06SA using a MAR CCD area detector and gave a data set with an overall Rmerge of 6.8% and a completeness of 91.1%.
El-Kabbani
Ossama
O
Department of Medicinal Chemistry, Victorian College of Pharmacy, Monash University, Parkville, Victoria 3052, Australia. ossama.el-kabbani@vcp.monash.edu.au
Ishikura
Syuhei
S
Wagner
Armin
A
Schulze-Briese
Clemens
C
Hara
Akira
A
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D018076:DNA, Complementary / Q000378:metabolism; D004058:Diffusion; D004926:Escherichia coli / Q000378:metabolism; D006913:Hydroxysteroid Dehydrogenases / Q000737:chemistry*; D051379:Mice; D011487:Protein Conformation; D020033:Protein Isoforms; D012997:Solvents; D014961:X-Ray Diffraction
D018076:DNA, Complementary; D020033:Protein Isoforms; D012997:Solvents; D006913:Hydroxysteroid Dehydrogenases; C035507:3(17)-hydroxysteroid dehydrogenase