Literature DB >> 15272169

Expression, purification, crystallization and preliminary X-ray diffraction data of methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis.

Hélène Dubourg1, Claire Stines-Chaumeil, Claude Didierjean, François Talfournier, Sophie Rahuel-Clermont, Guy Branlant, André Aubry.   

Abstract

Methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis was cloned and overexpressed in Escherichia coli. Suitable crystals for X-ray diffraction experiments were obtained by the hanging-drop vapour-diffusion method using ammonium sulfate as precipitant. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 195.2, b = 192.5, c = 83.5 A, and contain one tetramer per asymmetric unit. X-ray diffraction data were collected to 2.5 A resolution using a synchrotron-radiation source. The crystal structure was solved by the molecular-replacement method.

Entities:  

Mesh:

Substances:

Year:  2004        PMID: 15272169     DOI: 10.1107/S0907444904012533

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  2 in total

1.  Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis.

Authors:  Claire Stines-Chaumeil; François Talfournier; Guy Branlant
Journal:  Biochem J       Date:  2006-04-01       Impact factor: 3.857

2.  Adenine binding mode is a key factor in triggering the early release of NADH in coenzyme A-dependent methylmalonate semialdehyde dehydrogenase.

Authors:  Raphaël Bchini; Hélène Dubourg-Gerecke; Sophie Rahuel-Clermont; André Aubry; Guy Branlant; Claude Didierjean; François Talfournier
Journal:  J Biol Chem       Date:  2012-07-10       Impact factor: 5.157

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.