Crystallographic studies of cephalosporin acylase from Pseudomonas sp. strain 130
Tsinghua Science and Technology(2012)
摘要
The cephalosporin acylases are a group of enzymes that hydrolyze cephalosporin C and/or glutaryl 7-am nocephalosporanic acid to produce 7-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 O. 21 nm belonged to the space group P21. There was four αβheterodimers 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.
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关键词
diffraction (MAD),multiwavelength anomalous,heterotetramer,heterodimer,cephalospor in acylase,multiwavelength anomalous diffraction (mad),selenorrethionine (Se-Met),selenomethionine (se-met),cephalosporin acylase,crystallization
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