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The enzyme 3 (or 17) beta-hydroxysteroid dehydrogenase from Comamonas testosteroni was crystallized. Crystals, of up to 0.6 mm in their longest dimension and suitable for a crystallographic analysis have been obtained by the vapour diffusion method. They belong to the orthorhombic lattice type and diffract to a maximum resolution of 0.23 nm. A final data set obtained by merging data from three crystals resulted in a completeness of 90% with an Rmerge of 6%. A molecular replacement search carried out by using 3 alpha (or 20 beta)-hydroxysteroid dehydrogenase from Streptomyces hydrogenans as a search model allowed us to assign I222 as the correct space group and to propose a model for the crystal packing, with one monomer per asymmetric unit. Thus, the whole unit cell contains two tetramers. The R-factor after rigid body refinement is 48.1%.

Original publication

DOI

10.1111/j.1432-1033.1996.t01-1-00144.x

Type

Journal article

Journal

European journal of biochemistry

Publication Date

02/1996

Volume

236

Pages

144 - 148

Addresses

Karolinska Institutet, NOVUM, Center of Structural Biochemistry, Huddinge, Sweden.

Keywords

Gram-Negative Aerobic Bacteria, 3-Hydroxysteroid Dehydrogenases, 17-Hydroxysteroid Dehydrogenases, Recombinant Proteins, Crystallography, X-Ray, Amino Acid Sequence, Protein Conformation, Models, Molecular, Molecular Sequence Data