@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 = {<p>{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</p>},
	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.}
}
