| Title : Crystallization and preliminary X-ray diffraction analysis of proline iminopeptidase from Xanthomonas campestris pv. citri - Medrano_1997_FEBS.Lett_400_91 |
| Author(s) : Medrano FJ , Alonso J , Garcia JL , Bode W , Gomis-Ruth FX |
| Ref : FEBS Letters , 400 :91 , 1997 |
| Abstract : 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. |
| ESTHER : Medrano_1997_FEBS.Lett_400_91 |
| PubMedSearch : Medrano_1997_FEBS.Lett_400_91 |
| PubMedID: 9000519 |
| Gene_locus related to this paper: xanca-impep |
| Gene_locus related to this paper: xanca-impep |
Medrano FJ, Alonso J, Garcia JL, Bode W, Gomis-Ruth FX (1997)
Crystallization and preliminary X-ray diffraction analysis of proline iminopeptidase from Xanthomonas campestris pv. citri
FEBS Letters
400 :91
Medrano FJ, Alonso J, Garcia JL, Bode W, Gomis-Ruth FX (1997)
FEBS Letters
400 :91