3.4.19.3	-	95291, 95304, 95316	
3.4.19.3	crystal structure of wild-type and mutant enzyme C142S/C188S determined at 2.2 and 2.7 A resolution	651784	
3.4.19.3	crystallized from both ammonium phosphate and ammonium sulfate, structure determined at 1.7 A resolution	653129	
3.4.19.3	crystallographic analysis of enzyme-inhibitor complex with pyroglutaminal and of the mutant enzyme F142, hanging drop vapour diffusion method	652124	
3.4.19.3	hanging drop vapor diffusion method at 4°C, 1.6 A resolution	723069	
3.4.19.3	PCP-0SH polar mutants C142S/C188S/E192D andC142S/C188S/E192Q crystallize at a 6.5% PEG4000, while the apolar mutants C142S/C188S/E192A, C142S/C188S/E192I and C142S/C188S/E192V crystallize at a 5.7-6.0% PEG4000. The protein molecules crystallize in two different space groups. E192Q and E192V form isomorphic monoclinic crystals in the space group P2(1), which agree with those of the wild-type PCP and cysteine-free PCP-0SH (C142S/C188S), while E192A, E192D, and E192I form orthorhombic crystals in the space group P2(1)2(1)2(1). In both crystal systems, four subunit (monomer) molecules are contained in the asymmetric unit. A systematic analysis of individual structures indicates that the mutation does not have any significant effect on the overall structure	667733