Purification, crystallization and preliminary X-ray diffraction analysis of a variant of the ColE1 Rop protein.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 64(Pt 5): 432-4, 2008 May 01.
Article
em En
| MEDLINE
| ID: mdl-18453719
ABSTRACT
Rop is the paradigm of a canonical four-alpha-helical bundle. Its loop region has attracted considerable interest because a single alanine-to-proline substitution (A31P) in the loop is sufficient to change the topology of this small protein. In order to further analyse the loop region as a possible folding-control element, the double mutant D30P/A31G (RopPG) was produced, purified and crystallized. The crystals belonged to space group P2(1), with unit-cell parameters a = 26.7, b = 38.8, c = 56.6 A, beta = 100.9 degrees and two molecules in the asymmetric unit. A complete data set was collected at 100 K to a resolution of 1.4 A using synchrotron radiation.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Difração de Raios X
/
Proteínas de Ligação a RNA
/
Cristalização
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Ano de publicação:
2008
Tipo de documento:
Article
País de afiliação:
Grécia