Structures of an alanine racemase from Bacillus anthracis (BA0252) in the presence and absence of (R)-1-aminoethylphosphonic acid (L-Ala-P).

@article{Au2008StructuresOA,
  title={Structures of an alanine racemase from Bacillus anthracis (BA0252) in the presence and absence of (R)-1-aminoethylphosphonic acid (L-Ala-P).},
  author={Kinfai Au and Jingshan Ren and Thomas S Walter and Karl Harlos and Joanne E Nettleship and Raymond J. Owens and David I Stuart and Robert M. Esnouf},
  journal={Acta crystallographica. Section F, Structural biology and crystallization communications},
  year={2008},
  volume={64 Pt 5},
  pages={327-33}
}
Bacillus anthracis, the causative agent of anthrax, has been targeted by the Oxford Protein Production Facility to validate high-throughput protocols within the Structural Proteomics in Europe project. As part of this work, the structures of an alanine racemase (BA0252) in the presence and absence of the inhibitor (R)-1-aminoethylphosphonic acid (L-Ala-P) have determined by X-ray crystallography to resolutions of 2.1 and 1.47 A, respectively. Difficulties in crystallizing this protein were… CONTINUE READING
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