Crystallization and preliminary X-ray diffraction analysis of proline iminopeptidase from Xanthomonas campestris pv. citri.
Proline iminopeptidase from Xanthomonas campestris pv. citri, displaying no significant sequence homology to any protein previously analyzed by X-ray crystallography, has been crystallized using the vapour diffusion method. Two different orthorhombic crystal forms (space group C222 and I222) were obtained from a solution containing NaCl or polyethylene glycol monomethyl ether (MW 5000) as precipitating agent for the native and lanthanum-derivatized protein, respectively. Complete diffraction data sets have been collected up to 2.6 A (native) and 3.0 A (lanthanum derivative) resolution. Cell dimensions are a= 147.2 A, b = 167.8 A, and c = 85.6 A (C222) and a = 146.7 A, b = 167.7 A, and c = 171.4 A (I222), respectively. Considerations of the possible values of V(m) and analysis of the self-rotation function of the native crystals account for the presence of one dimer per asymmetric unit, whereas a tetramer probably would occupy the smallest crystallographically independent crystal portion in the lanthanum-derivatized protein crystals.
Medrano
F J
FJ
Max-Planck-Institut für Biochemie, Abteilung Structurforschung, Martinsreid, Germany. medrano@alf.biochem.mpg.de
Alonso
J
J
García
J L
JL
Bode
W
W
Gomis-Rüth
F X
FX
D000626:Aminopeptidases / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D016959:Xanthomonas campestris / Q000201:enzymology*
D011994:Recombinant Proteins; D000626:Aminopeptidases; C022450:prolyl aminopeptidase