Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 64, Part 5 (May 2008)

crystallization communications

Acta Cryst. (2008). F64, 394-397 [ doi:10.1107/S1744309108008579 ]

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

Supangat, K. H. Seo, A. Furqoni, Y.-C. Kwon, M.-J. Cho, K.-H. Rhee, S. Y. Lee and K. H. Lee

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 Å resolution and belonged to space group C2, with unit-cell parameters a = 245.8, b = 140.7, c = 189.5 Å, [beta] = 127°, 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 Å resolution. It belonged to space group C222, with unit-cell parameters a = 257.5, b = 417.5, c = 95.6 Å. The structure of the monomeric form of C49S HpAhpC has been solved by the molecular-replacement method.

Keywords: alkyl hydroperoxide reductases; Helicobacter pylori; cysteine mutant.