Crystallization and preliminary X-ray analysis of outer membrane phospholipase A from Escherichia coli.
FEBS Lett
; 373(1): 10-2, 1995 Oct 02.
Article
en En
| MEDLINE
| ID: mdl-7589423
ABSTRACT
The outer membrane phospholipase A (OMPLA) of Escherichia coli is one of the few integral outer membrane proteins displaying enzymatic activity. It is encoded as a mature protein of 269 amino acids preceded by a signal sequence of 20 amino acids. There is no sequence homology with water-soluble lipases and phospholipases. Crystals of the mature enzyme were obtained at 22 degrees C from 24-28% (v/v) 2-methyl-2,4-pentanediol in Bis-Tris buffer, pH 5.9-6.0, with 1 mM calcium chloride and 1.5% (w/v) beta-octylglucoside. They have the symmetry of the trigonal spacegroup P3(1)21 (or P3(2)21) with cell dimensions of a = b = 79.6 A and c = 102.8 A (alpha = beta = 90 degrees, gamma = 120 degrees). Native crystals diffract to a resolution of 2.6 A.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Fosfolipasas A
/
Escherichia coli
Idioma:
En
Revista:
FEBS Lett
Año:
1995
Tipo del documento:
Article
País de afiliación:
Países Bajos