@article { ISI:000232157000036,
	title = {Cloning, preparation and preliminary crystallographic studies of penicillin V acylase autoproteolytic processing mutants},
	journal = {Acta Crystallographica Section F-Structural Biology and Crystallization Communications},
	volume = {61},
	number = {1},
	year = {2005},
	month = {JAN},
	pages = {124-127},
	publisher = {BLACKWELL PUBLISHING},
	type = {Article},
	address = {9600 GARSINGTON RD, OXFORD OX4 2DQ, OXON, ENGLAND},
	issn = {1744-3091},
	doi = {10.1107/S1744309104031227},
	author = {Chandra, P. M. and Brannigan, James A. and Prabhune, Asmita and Pundle, A. and Turkenburg, J. P. and Dodson, Guy G. and Suresh, C. G.}
}
@article { ISI:000232320400015,
	title = {Cloning, purification, crystallization and preliminary structural studies of penicillin V acylase from Bacillus subtilis},
	journal = {Acta Crystallographica Section F-Structural Biology Communications},
	volume = {61},
	number = {7},
	year = {2005},
	month = {JUL},
	pages = {680-683},
	publisher = {INT UNION CRYSTALLOGRAPHY},
	type = {Article},
	address = {2 ABBEY SQ, CHESTER, CH1 2HU, ENGLAND},
	abstract = {<p>{Penicillin acylase proteins are amidohydrolase enzymes that cleave penicillins at the amide bond connecting the side chain to their beta-lactam nucleus. An unannotated protein from Bacillus subtilis has been expressed in Escherichia coli, purified and confirmed to possess penicillin V acylase activity. The protein was crystallized using the hanging-drop vapour-diffusion method from a solution containing 4 M sodium formate in 100 mM Tris-HCl buffer pH 8.2. Diffraction data were collected under cryogenic conditions to a spacing of 2.5 A. The crystals belonged to the orthorhombic space group C222(1), with unit-cell parameters a = 111.0</p>},
	issn = {2053-230X},
	author = {Rathinaswamy, P. and Pundle, A. V. and Prabhune, Asmita and SivaRaman, H. and Brannigan, James A. and Dodson, Guy G. and Suresh, C. G.}
}
