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Crystallization and preliminary X-ray analysis of the hypothetical deaminase RPB_0146 from Rhodopseudomonas palustris HaA2.

ABSTRACT: RPB_0146, a putative deaminase from Rhodopseudomonas palustris HaA2, was expressed in Escherichia coli BL21 (DE3) cells and purified using a His6 tag by Ni2+-chelating affinity chromatography for X-ray crystallographic analysis. Diffraction-quality crystals were grown by the hanging-drop vapour-diffusion method at 289?K and diffracted to a resolution of 2.44?Å using a wavelength of 1.000?Å at the Photon Factory (KEK), Japan. The crystals belonged to the orthorhombic space group P2?2?2?, with unit-cell parameters a=66.26, b=123.94, c=155.95?Å.

SUBMITTER: Zhang G 

PROVIDER: S-EPMC4231866 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of the hypothetical deaminase RPB_0146 from Rhodopseudomonas palustris HaA2.

Zhang Guofang G   Yu Dan D   Yang Guodong G   Dong Hui H   Zhang Tongcun T   Liu Xiang X  

Acta crystallographica. Section F, Structural biology communications 20141031 Pt 11

RPB_0146, a putative deaminase from Rhodopseudomonas palustris HaA2, was expressed in Escherichia coli BL21 (DE3) cells and purified using a His6 tag by Ni2+-chelating affinity chromatography for X-ray crystallographic analysis. Diffraction-quality crystals were grown by the hanging-drop vapour-diffusion method at 289 K and diffracted to a resolution of 2.44 Å using a wavelength of 1.000 Å at the Photon Factory (KEK), Japan. The crystals belonged to the orthorhombic space group P2₁2₁2₁, with uni  ...[more]

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