Crystallization and preliminary X-ray analysis ofEscherichia colip20, a novel thiol peroxidase
| Autor: | Jongkeun Choi, Soonwoong Choi, Mee-Kyung Cha, Jung Won Choi, Il-Han Kim, Whanchul Shin |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Stereochemistry
Crystallography X-Ray medicine.disease_cause law.invention Structural Biology law PEG ratio Escherichia coli medicine Crystallization chemistry.chemical_classification biology Reverse Transcriptase Polymerase Chain Reaction Escherichia coli Proteins General Medicine Recombinant Proteins Solvent Enzyme Peroxidases chemistry biology.protein Thiol Orthorhombic crystal system Periplasmic Proteins Peroxidase |
| Zdroj: | Acta Crystallographica Section D Biological Crystallography. 59:1064-1066 |
| ISSN: | 0907-4449 |
| DOI: | 10.1107/s0907444903006930 |
| Popis: | Escherichia coli p20 is a thioredoxin-dependent thiol peroxidase. This protein represents a novel group of antioxidant enzymes that are widely expressed in various pathogenic bacteria and show distant yet significant sequence homology with peroxiredoxins. E. coli p20, overexpressed in E. coli, was crystallized with PEG 4000 and 2-propanol as precipitants using the hanging-drop vapour-diffusion method. Diffraction data were collected to 2.2 A resolution using synchrotron radiation. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 38.97, b = 58.97, c = 127.59 A. The asymmetric unit contains two p20 molecules, with a corresponding V(M) of 2.06 A(3) Da(-1) and a solvent content of 40.4%. |
| Databáze: | OpenAIRE |
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