Crystallization and preliminary crystallographic analysis of decameric and monomeric forms of C49S mutant thioredoxin-dependent AhpC from Helicobacter pyloriopen access
- Authors
- Supangat; Seo, Kyung Hye; Furqoni, Ahmad; Kwon, Young-Chul; Cho, Myung-Je; Rhee, Kwang-Ho; Lee, Sang Yeol; Lee, Kon Ho
- Issue Date
- May-2008
- Publisher
- INT UNION CRYSTALLOGRAPHY
- Keywords
- Alkyl hydroperoxide reductases; Cysteine mutant; Helicobacter pylori
- Citation
- ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.64, pp.394 - 397
- Indexed
- SCIE
SCOPUS
- Journal Title
- ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
- Volume
- 64
- Start Page
- 394
- End Page
- 397
- URI
- https://scholarworks.bwise.kr/gnu/handle/sw.gnu/27421
- DOI
- 10.1107/S1744309108008579
- 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 angstrom resolution and belonged to space group C2, with unit-cell parameters a = 245.8, b = 140.7, c = 189.5 angstrom, 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 angstrom resolution. It belonged to space group C222, with unit-cell parameters a = 257.5, b = 417.5, c = 95.6 angstrom. The structure of the monomeric form of C49S HpAhpC has been solved by the molecular-replacement method.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - College of Medicine > Department of Medicine > Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.gnu.ac.kr/handle/sw.gnu/27421)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.