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Title: Improved X-ray diffraction from Bacillus megaterium penicillin G acylase crystals through long cryosoaking dehydration
Authors: Catleya Rojviriya
Thunyaluck Pratumrat
Mark A. Saper
Jirundon Yuvaniyama
Mahidol University
University Michigan Ann Arbor
Keywords: Biochemistry, Genetics and Molecular Biology;Physics and Astronomy
Issue Date: 1-Dec-2011
Citation: Acta Crystallographica Section F: Structural Biology and Crystallization Communications. Vol.67, No.12 (2011), 1570-1574
Abstract: Penicillin G acylase from Bacillus megaterium (BmPGA) is currently used in the pharmaceutical industry as an alternative to PGA from Escherichia coli (EcPGA) for the hydrolysis of penicillin G to produce 6-aminopenicillanic acid (6-APA), a penam nucleus for semisynthetic penicillins. Despite the significant differences in amino-acid sequence between PGAs from Gram-positive and Gram-negative bacteria, a representative PGA structure of Gram-positive origin has never been reported. In this study, crystallization and diffraction studies of BmPGA are described. Poor diffraction patterns with blurred spots at higher resolution were typical for BmPGA crystals cryocooled after a brief immersion in cryoprotectant solution. Overnight soaking in the same cryo-solution substantially improved both the mosaicity and resolution limit through the establishment of a new crystal-packing equilibrium. A crystal of BmPGA diffracted X-rays to 2.20 Å resolution and belonged to the monoclinic space group P21 with one molecule of BmPGA in the asymmetric unit. © 2011 International Union of Crystallography. All rights reserved.
ISSN: 17443091
Appears in Collections:Scopus 2011-2015

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