Putative thioredoxin Trx1 from Thermosipho africanus strain TCF52B: expression, purification and structural determination using S-SAD.
Acta Crystallogr F Struct Biol Commun
; 72(Pt 6): 443-7, 2016 06.
Article
en En
| MEDLINE
| ID: mdl-27303896
ABSTRACT
Thioredoxin is a small ubiquitous protein that plays a role in many biological processes. A putative thioredoxin, Trx1, from Thermosipho africanus strain TCF52B, which has low sequence identity to its closest homologues, was successfully cloned, overexpressed and purified. The protein was crystallized using the microbatch-under-oil technique at 289â
K in a variety of conditions; crystals grown in 0.2â
M MgCl2, 0.1â
M bis-tris pH 6.5, 25%(w/v) PEG 3350, which grew as irregular trapezoids to maximum dimensions of 1.2 × 1.5 × 0.80â
mm, were used for sulfur single-wavelength anomalous dispersion analysis. The anomalous sulfur signal could be detected to 2.83â
Å resolution using synchrotron radiation on the 08B1-1 beamline at the Canadian Light Source. The crystals belonged to space group P212121, with unit-cell parameters a = 40.6, b = 41.5, c = 56.4â
Å, α = ß = γ = 90.0°.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Tiorredoxinas
/
Bacterias
/
Proteínas Bacterianas
Idioma:
En
Revista:
Acta Crystallogr F Struct Biol Commun
Año:
2016
Tipo del documento:
Article
País de afiliación:
Canadá