Cloning, purification and crystallographic analysis of a hypothetical protein, BPSL1549, from Burkholderia pseudomallei
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Published:2011-11-30
Issue:12
Volume:67
Page:1623-1626
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ISSN:1744-3091
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Container-title:Acta Crystallographica Section F Structural Biology and Crystallization Communications
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language:
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Short-container-title:Acta Cryst Sect F
Author:
Cruz-Migoni Abimael,Ruzheinikov Sergey N.,Sedelnikova Svetlana E.,Obeng Barbara,Chieng Sylvia,Mohamed Rahmah,Nathan Sheila,Baker Patrick J.,Rice David W.
Abstract
Burkholderia pseudomallei BPSL1549, a putative protein of unknown function, has been overexpressed in Escherichia coli, purified and subsequently crystallized by the hanging-drop vapour-diffusion method using PEG as a precipitant to give crystals with overall dimensions of 0.15 × 0.15 × 0.1 mm. Native data were collected to 1.47 Å resolution at the European Synchrotron Radiation Facility (ESRF). The crystals belonged to space group P212121, with unit-cell parameters a = 37.1, b = 45.4, c = 111.9 Å and with a single polypeptide chain in the asymmetric unit.
Publisher
International Union of Crystallography (IUCr)
Subject
Condensed Matter Physics,Genetics,Biochemistry,Structural Biology,Biophysics
Cited by
2 articles.
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1. Structural Genomics;Encyclopedia of Bioinformatics and Computational Biology;2019
2. Crystals on the cover 2012;Acta Crystallographica Section F Structural Biology and Crystallization Communications;2011-12-24