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Crystallization and preliminary X-ray diffraction analysis of alanine racemase from Pseudomonas putida YZ-26.


ABSTRACT: A recombinant form of alanine racemase (Alr) from Pseudomonas putida YZ-26 has been crystallized by the sitting-drop vapour diffusion method. X-ray diffraction data were collected to 2.4?Å resolution. The crystals belong to the space group C222(1), with unit-cell parameters a = 118.08, b = 141.86, c = 113.83?Å, and contain an Alr dimer in the asymmetric unit. The Matthews coefficient and the solvent content were calculated to be 2.8?Å(3)?Da(-1) and approximately 50%, respectively.

SUBMITTER: Liu J 

PROVIDER: S-EPMC3497987 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of alanine racemase from Pseudomonas putida YZ-26.

Liu Junlin J   Feng Lei L   Shi Yawei Y   Feng Wei W  

Acta crystallographica. Section F, Structural biology and crystallization communications 20120929 Pt 10


A recombinant form of alanine racemase (Alr) from Pseudomonas putida YZ-26 has been crystallized by the sitting-drop vapour diffusion method. X-ray diffraction data were collected to 2.4 Å resolution. The crystals belong to the space group C222(1), with unit-cell parameters a = 118.08, b = 141.86, c = 113.83 Å, and contain an Alr dimer in the asymmetric unit. The Matthews coefficient and the solvent content were calculated to be 2.8 Å(3) Da(-1) and approximately 50%, respectively. ...[more]

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