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Crystallization and preliminary X-ray diffraction analysis of cyclic imide hydrolase (CIH) from Pseudomonas putida YZ-26.


ABSTRACT: A recombinant form of cyclic imide hydrolase from Pseudomonas putida YZ-26 has been crystallized by the hanging-drop method. X-ray diffraction data were collected to 1.9?Å resolution. The crystals belonged to the orthorhombic space group C222(1), with unit-cell parameters a = 111.91, b = 176.04, c = 176.06?Å. Assuming the presence of four molecules in the asymmetric unit gives a V(M) value of 3.10?Å(3)?Da(-1) and a solvent content of 60.31%.

SUBMITTER: Fan Z 

PROVIDER: S-EPMC3080166 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of cyclic imide hydrolase (CIH) from Pseudomonas putida YZ-26.

Fan Zheng Z   Qi Jianxun J   Shi Yawei Y   Liu Yiwei Y  

Acta crystallographica. Section F, Structural biology and crystallization communications 20110330 Pt 4


A recombinant form of cyclic imide hydrolase from Pseudomonas putida YZ-26 has been crystallized by the hanging-drop method. X-ray diffraction data were collected to 1.9 Å resolution. The crystals belonged to the orthorhombic space group C222(1), with unit-cell parameters a = 111.91, b = 176.04, c = 176.06 Å. Assuming the presence of four molecules in the asymmetric unit gives a V(M) value of 3.10 Å(3) Da(-1) and a solvent content of 60.31%. ...[more]

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