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

Authors: Otagiri M.; Kurisu G.; Ui S.; Ohkum M.; Kudo T.; Kusunoki M.

Source: Protein and Peptide Letters, Volume 8, Number 1, February 2001 , pp. 57-61(5)

Publisher: Bentham Science Publishers

Buy & download fulltext article:

Price: $63.10 plus tax (Refund Policy)

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

Keywords: BUTANEDIOL DEHYDROGENASE; BREVIBACTERIUM SACCHAROLYTICUM; Klebsiella pneumoniae; Bacillus polymyxa; Serratia marcescens; Three-dimensional structures

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866013409670

Publication date: 2001-02-01

More about this publication?

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.