@article { ISI:000301921300006, title = {Crystallization and X-ray structure analysis of a thermostable penicillin G acylase from alcaligenes faecalis}, journal = {Acta Crystallographica Section F-Structural Biology and Crystallization Communications}, volume = {68}, number = {3}, year = {2012}, month = {MAR}, pages = {273-277}, publisher = {WILEY-BLACKWELL}, address = {COMMERCE PLACE, 350 MAIN ST, MALDEN 02148, MA USA}, abstract = {

{The enzyme penicillin G acylase (EC 3.5.1.11) catalyzes amide-bond cleavage in benzylpenicillin (penicillin G) to yield 6-aminopenicillanic acid, an intermediate chemical used in the production of semisynthetic penicillins. A thermostable penicillin G acylase from Alcaligenes faecalis (AfPGA) has been crystallized using the hanging-drop vapour-diffusion method in two different space groups: C2221, with unit-cell parameters a = 72.9

}, keywords = {calcium binding, disulfide bridges, Ntn hydrolases, orthorhombic form, tetragonal form, Thermostability}, issn = {1744-3091}, doi = {10.1107/S1744309111053930}, author = {Varshney, Nishant Kumar and Kumar, R. Suresh and Ignatova, Zoya and Prabhune, Asmita and Pundle, Archana and Dodson, Eleanor J. and Suresh, C. G.} }