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 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.
Mistou
M Y
MY
Unité d'Enzymologie, INRA Centre de Recherches de Jouy en Josas, France.
Rigolet
P
P
Chapot-Chartier
M P
MP
Nardi
M
M
Gripon
J C
JC
Brunie
S
S
D000626:Aminopeptidases / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D003546:Cysteine Endopeptidases / Q000737:chemistry; D013294:Lactococcus lactis / Q000201:enzymology*
D000626:Aminopeptidases; C086319:PepC thiol aminopeptidase; D003546:Cysteine Endopeptidases; C031262:bleomycin hydrolase