title: Crystallization and preliminary X-ray analysis of PepC, a thiol aminopeptidase from Lactoccocus lactis homologous to bleomycin hydrolase.
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.
authors.affiliation: Unité d'Enzymologie, INRA Centre de Recherches de Jouy en Josas, France.
authors.forename: M Y
authors.initials: MY
authors.lastname: Mistou
authors.forename: P
authors.initials: P
authors.lastname: Rigolet
authors.forename: M P
authors.initials: MP
authors.lastname: Chapot-Chartier
authors.forename: M
authors.initials: M
authors.lastname: Nardi
authors.forename: J C
authors.initials: JC
authors.lastname: Gripon
authors.forename: S
authors.initials: S
authors.lastname: Brunie
mesh_terms: D000626:Aminopeptidases / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D003546:Cysteine Endopeptidases / Q000737:chemistry; D013294:Lactococcus lactis / Q000201:enzymology*
chemical_list: D000626:Aminopeptidases; C086319:PepC thiol aminopeptidase; D003546:Cysteine Endopeptidases; C031262:bleomycin hydrolase