Crystallization and preliminary X-ray analysis of PepC, a thiol aminopeptidase from Lactoccocus lactis homologous to bleomycin hydrolase.
J Mol Biol
; 237(1): 160-2, 1994 Mar 18.
Article
em En
| MEDLINE
| ID: mdl-8133515
ABSTRACT
Crystals of the recombinant thiol aminopeptidase PepC, from Lactoccocus lactis, have been obtained using the hanging-drop method of vapor diffusion from ammonium sulfate solutions. Crystals are rhombohedral, the space group is R32, a = 175.2 A, c = 94.5 A (hexagonal setting). The asymmetric unit probably contains one monomer of a hexameric molecule-arrangement of 300 kDa which exhibits the crystallographic point group of symmetry 32. The crystals diffract to at least 3 A resolution.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Lactococcus lactis
/
Aminopeptidases
Idioma:
En
Revista:
J Mol Biol
Ano de publicação:
1994
Tipo de documento:
Article
País de afiliação:
França