Crystallization and crystal packing of recombinant 3 (or 17) beta-hydroxysteroid dehydrogenase from Comamonas testosteroni ATTC 11996.

Journal article

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%.

Authors: Benach, J; Knapp, S; Oppermann, U; Hägglund, O; Jörnvall, H

• Publisher: Blackwell Publishing Ltd
• Journal: European journal of biochemistry / FEBS
• Volume: 236
• Issue: 1
• Pages: 144-148
• Publication date: 1996-02-01
• DOI: 10.1111/j.1432-1033.1996.t01-1-00144.x
• EISSN: 1432-1033
• ISSN: 0014-2956
• Language: English
• Keywords: 3-Hydroxysteroid Dehydrogenases; Molecular Sequence Data; Crystallography, X-Ray; Amino Acid Sequence; Protein Conformation; Recombinant Proteins; Gram-Negative Aerobic Bacteria; 17-Hydroxysteroid Dehydrogenases; Models, Molecular