Crystallization and preliminary X-ray study of alkaline alanine racemase from Bacillus pseudofirmus OF4. Academic Article

abstract

• Alanine racemase (DadX(OF4)), a dimeric endogenous PLP-dependent alkaline enzyme from alkaliphilic Bacillus pseudofirmus OF4, was expressed in Escherichia coli and purified with a His(6) tag in a form suitable for X-ray crystallographic analysis. Crystals were grown by the hanging-drop vapour-diffusion method at 291 K using a solution containing 1.4 M sodium/potassium phosphate pH 8.2. The protein crystallized in space group P2(1)2(1)2(1), with two protein molecules in the asymmetric unit.

authors

• Benedik, Michael

published proceedings

• Acta Crystallogr Sect F Struct Biol Cryst Commun

author list (cited authors)

• Ju, J., Qi, J., Xu, S., Ohnishi, K., Benedik, M. J., Xue, Y., & Ma, Y.

citation count

• 3

complete list of authors

• Ju, Jiansong||Qi, Jianxun||Xu, Shujing||Ohnishi, Kouhei||Benedik, Michael J||Xue, Yanfen||Ma, Yanhe

publication date

• February 2009

publisher

• International Union of Crystallography (IUCr)  Publisher

keywords

• Alanine Racemase
• Bacillus
• Crystallization
• Crystallography, X-Ray
• Hydrogen-Ion Concentration

Digital Object Identifier (DOI)

• 10.1107/S174430910900013X

start page

• 166

end page

• 168

volume

• 65

issue

• Pt 2

URL

• http://dx.doi.org/10.1107/s174430910900013x