Crystallographic Studies of Cephalosporin Acylase from Pseudomonas sp. Strain 130

The cephalosporin acylases are a group of enzymes that hydrolyze cephalosporin C and/or glutaryl 7-aminocephalosporanic acid to produce ?-aminocephalosporanic acid. The cephalosporin acylase from Pseudomonas sp. strain 130 was crystallized in two different forms suitable for structural studies. A tetragonal crystal form diffracted to 0.24 nm belonged to the space group P41212. There was one αβ heterodimer per asymmetric unit. A second crystal form diffracted to 0.21nm belonged to the space group P21. There was four αβ heterodimers per asymmetric unit. The tetragonal crystal structure of CA-130 was determined using the multiwavelength anomalous diffraction method and the P21 crystal structure was then determined using the molecular replacement method.