Crystallization and preliminary X-ray diffraction analysis of mouse 3(17)alpha-hydroxysteroid dehydrogenase

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Ossama El-KabbaniAkira Hara

Abstract

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%.

References

Jul 1, 1990·Acta Crystallographica. Section A, Foundations of Crystallography·A T BrüngerJ W Erickson
Apr 28, 1968·Journal of Molecular Biology·B W Matthews

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Citations

Oct 3, 2007·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Urmi DhagatOssama El-Kabbani

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