Crystallization and preliminary X-ray analysis of a truncated mutant of yeast nuclear thiol peroxidase, a novel atypical 2-Cys peroxiredoxin.

Autor: Jongkeun Choi, Soonwoong Choi, Jungwon Choi, Mee-Kyung Cha, Il-Han Kim, Whanchul Shina
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Zdroj: Acta Crystallographica: Section F (Wiley-Blackwell); Jul2005, Vol. 61 Issue 7, p659-662, 4p
Abstrakt: Saccharomyces cerevisiae nTPx is a thioredoxin-dependent thiol peroxidase that is localized in the nucleus. nTPx belongs to the C-type atypical 2-Cys peroxiredoxin family members, which are frequently called BCPs or PrxQs. A double mutant (C107S/C112S) of nTPx overexpressed in Escherichia coli was spontaneously degraded upon freezing and thawing and its truncated form (residues 57–215; MW = 17837 Da) was crystallized with PEG 3350 and mercury(II) acetate as precipitants using the hanging-drop vapour-diffusion method. Diffraction data were collected to 1.8 Å resolution using X-ray synchrotron radiation. The crystals belong to the trigonal space group P32, with unit-cell parameters a = b = 37.54, c = 83.26 Å. The asymmetric unit contains one molecule of truncated mutant nTPx, with a corresponding VM of 1.91 Å3 Da−1 and a solvent content of 35.5%. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index