Crystallization and preliminary X-ray analysis of PepC, a thiol aminopeptidase from Lactoccocus lactis homologous to bleomycin hydrolase

Crystallization and preliminary X-ray analysis of PepC, a thiol aminopeptidase from Lactoccocus lactis homologous to bleomycin hydrolase

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 pro...

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Bibliographic Details
Published in:Journal of molecular biology Vol. 237; no. 1; p. 160
Main Authors: Mistou, M Y, Rigolet, P, Chapot-Chartier, M P, Nardi, M, Gripon, J C, Brunie, S
Format: Journal Article
Language:English
Published: England 18-03-1994
Subjects:
Aminopeptidases - chemistry
Crystallization
Crystallography, X-Ray
Cysteine Endopeptidases - chemistry
Lactococcus lactis - enzymology
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Summary: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.
ISSN:0022-2836
DOI:10.1006/jmbi.1994.1215