Crystallization and preliminary X-ray analysis of a truncated mutant of yeast nuclear thiol peroxidase, a novel atypical 2-Cys peroxiredoxin
| Autor: | Soonwoong Choi, Jongkeun Choi, Mee-Kyung Cha, Jung Won Choi, Whanchul Shin, Il-Han Kim |
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| Rok vydání: | 2005 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Saccharomyces cerevisiae Mutant Biophysics Crystallography X-Ray medicine.disease_cause Polymerase Chain Reaction Biochemistry Polyethylene Glycols Diffusion Thioredoxins X-Ray Diffraction Structural Biology Escherichia coli Genetics medicine Cysteine chemistry.chemical_classification biology X-Rays Mercury Peroxiredoxins Condensed Matter Physics biology.organism_classification Yeast Protein Structure Tertiary Crystallography Peroxidases chemistry Crystallization Communications Mutation Solvents Thiol biology.protein Peroxiredoxin Synchrotrons Peroxidase |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61:659-662 |
| ISSN: | 1744-3091 |
| DOI: | 10.1107/s1744309105016970 |
| Popis: | 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 A resolution using X-ray synchrotron radiation. The crystals belong to the trigonal space group P3(2), with unit-cell parameters a = b = 37.54, c = 83.26 A. The asymmetric unit contains one molecule of truncated mutant nTPx, with a corresponding VM of 1.91 A3 Da(-1) and a solvent content of 35.5%. |
| Databáze: | OpenAIRE |
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