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Crystallization and preliminary crystallographic analysis of decameric and monomeric forms of C49S mutant thioredoxin-dependent AhpC from Helicobacter pylori.


ABSTRACT: Cys49Ser mutant Helicobacter pylori alkyl hydroperoxide reductase (C49S HpAhpC) was purified under reducing conditions in monomeric and decameric forms. The monomeric form was crystallized by the hanging-drop vapour-diffusion method. The crystals diffracted to 2.25 A resolution and belonged to space group C2, with unit-cell parameters a = 245.8, b = 140.7, c = 189.5 A, beta = 127 degrees , and contained 20 molecules in the asymmetric unit. A crystal of the decameric form was obtained by the microbatch crystallization method and diffracted to 2.8 A resolution. It belonged to space group C222, with unit-cell parameters a = 257.5, b = 417.5, c = 95.6 A. The structure of the monomeric form of C49S HpAhpC has been solved by the molecular-replacement method.

SUBMITTER: Supangat 

PROVIDER: S-EPMC2376400 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature

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Crystallization and preliminary crystallographic analysis of decameric and monomeric forms of C49S mutant thioredoxin-dependent AhpC from Helicobacter pylori.

Seo Kyung Hye KH   Furqoni Ahmad A   Kwon Young Chul YC   Cho Myung Je MJ   Rhee Kwang Ho KH   Lee Sang Yeol SY   Lee Kon Ho KH  

Acta crystallographica. Section F, Structural biology and crystallization communications 20080405 Pt 5


Cys49Ser mutant Helicobacter pylori alkyl hydroperoxide reductase (C49S HpAhpC) was purified under reducing conditions in monomeric and decameric forms. The monomeric form was crystallized by the hanging-drop vapour-diffusion method. The crystals diffracted to 2.25 A resolution and belonged to space group C2, with unit-cell parameters a = 245.8, b = 140.7, c = 189.5 A, beta = 127 degrees , and contained 20 molecules in the asymmetric unit. A crystal of the decameric form was obtained by the micr  ...[more]

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