<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Varshney, Nishant Kumar</style></author><author><style face="normal" font="default" size="100%">Kumar, R. Suresh</style></author><author><style face="normal" font="default" size="100%">Ignatova, Zoya</style></author><author><style face="normal" font="default" size="100%">Prabhune, Asmita</style></author><author><style face="normal" font="default" size="100%">Pundle, Archana</style></author><author><style face="normal" font="default" size="100%">Dodson, Eleanor J.</style></author><author><style face="normal" font="default" size="100%">Suresh, C. G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Crystallization and X-ray structure analysis of a thermostable penicillin G acylase from alcaligenes faecalis</style></title><secondary-title><style face="normal" font="default" size="100%">Acta Crystallographica Section F-Structural Biology and Crystallization Communications</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">calcium binding</style></keyword><keyword><style  face="normal" font="default" size="100%">disulfide bridges</style></keyword><keyword><style  face="normal" font="default" size="100%">Ntn hydrolases</style></keyword><keyword><style  face="normal" font="default" size="100%">orthorhombic form</style></keyword><keyword><style  face="normal" font="default" size="100%">tetragonal form</style></keyword><keyword><style  face="normal" font="default" size="100%">Thermostability</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2012</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAR</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><publisher><style face="normal" font="default" size="100%">WILEY-BLACKWELL</style></publisher><pub-location><style face="normal" font="default" size="100%">COMMERCE PLACE, 350 MAIN ST, MALDEN 02148, MA USA</style></pub-location><volume><style face="normal" font="default" size="100%">68</style></volume><pages><style face="normal" font="default" size="100%">273-277</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;{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&lt;/p&gt;</style></abstract><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">0.552
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