Citation
Shaibullah, Sofiyah and Mohd Sharif, Nurhikmah and Ho, Kok Lian and Raih, Mohd Firdaus and Nathan, Sheila and Mohamed, Rahmah and Ng, Chyan Leong
(2014)
Crystallization and preliminary crystallographic studies of the hypothetical protein BPSL 1038 from Burkholderia pseudomallei.
Acta Crystallographica. Section F: Structural Biology Communications, 70 (12).
pp. 1697-1700.
ISSN 2053-230X
Abstract
Melioidosis is an infectious disease caused by the pathogenic bacterium Burkholderia pseudomallei. Whole-genome sequencing revealed that the B. pseudomallei genome includes 5855 coding DNA sequences (CDSs), of which ∼25% encode hypothetical proteins. A pathogen-associated hypothetical protein, BPSL1038, was overexpressed in Escherichia coli, purified and crystallized using vapour-diffusion methods. A BPSL1038 protein crystal that grew using sodium formate as precipitant diffracted to 1.55 Å resolution. It belonged to space group C2221, with unit-cell parameters a = 85.36, b = 115.63, c = 46.73 Å. The calculated Matthews coefficient (VM) suggests that there are two molecules per asymmetric unit, with a solvent content of 48.8%.
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Crystallization and preliminary crystallographic studies of the hypothetical protein BPSL 1038 from Burkholderia pseudomallei.pdf
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