Crystallization And Preliminary X-Ray Studies Of L-(+)-2,3-Butanediol Dehydrogenase From Brevibacterium Saccharolyticum C-1012

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Abstract:

L(+)-2,3 -Butanediol dehydrogenase (L-BDH) from Brevibacterium saccharolyticum C-1012 has been crystallized by the hanging drop vapor diffusion method with polyethylene glycol 4000 as the precipitant. Crystals of L-BDH belong to the triclinic system, space group P1 with cell dimensions a = 60.8 A, b = 69.2 A, c = 127.4 A , alpha = 96.1 , beta = 100.2 and gama=109.6 . Crystals diffracted to 2.0 A resolution on a synchrotron radiation, and a full data set was collected at resolution of 2.0 A at 100K.c
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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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