Crystallization and preliminary crystallographic studies of the hypothetical protein BPSL1038 from Burkholderia pseudomallei

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, BP...

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Main Authors: Shaibullah, Sofiyah, Mohd-Sharif, Nurhikmah, Ho, Kok Lian, Raih, Mohd Firdaus, Nathan, Sheila, Rahmah, Mohamed, Ng, Chyan Leong
Format: Article
Language:English
Published: International Union of Crystallography 2014
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Online Access:http://eprints.intimal.edu.my/156/
http://eprints.intimal.edu.my/156/1/Crystallization%20and%20preliminary%20crystallographic%20studies%20of%20the%20hypothetical%20protein%20BPSL1038%20from%20Burkholderia%20pseudomallei.pdf
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author Shaibullah, Sofiyah
Mohd-Sharif, Nurhikmah
Ho, Kok Lian
Raih, Mohd Firdaus
Nathan, Sheila
Rahmah, Mohamed
Ng, Chyan Leong
author_facet Shaibullah, Sofiyah
Mohd-Sharif, Nurhikmah
Ho, Kok Lian
Raih, Mohd Firdaus
Nathan, Sheila
Rahmah, Mohamed
Ng, Chyan Leong
author_sort Shaibullah, Sofiyah
building INTI Institutional Repository
collection Online Access
description 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 A ° resolution. It belonged to space group C2221, with unit-cell parameters a = 85.36, b = 115.63, c = 46.73 A ° . 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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spelling intimal-1562017-03-03T01:49:33Z http://eprints.intimal.edu.my/156/ Crystallization and preliminary crystallographic studies of the hypothetical protein BPSL1038 from Burkholderia pseudomallei Shaibullah, Sofiyah Mohd-Sharif, Nurhikmah Ho, Kok Lian Raih, Mohd Firdaus Nathan, Sheila Rahmah, Mohamed Ng, Chyan Leong TP Chemical technology 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 A ° resolution. It belonged to space group C2221, with unit-cell parameters a = 85.36, b = 115.63, c = 46.73 A ° . The calculated Matthews coefficient (VM) suggests that there are two molecules per asymmetric unit, with a solvent content of 48.8%. International Union of Crystallography 2014 Article PeerReviewed text en http://eprints.intimal.edu.my/156/1/Crystallization%20and%20preliminary%20crystallographic%20studies%20of%20the%20hypothetical%20protein%20BPSL1038%20from%20Burkholderia%20pseudomallei.pdf Shaibullah, Sofiyah and Mohd-Sharif, Nurhikmah and Ho, Kok Lian and Raih, Mohd Firdaus and Nathan, Sheila and Rahmah, Mohamed and Ng, Chyan Leong (2014) Crystallization and preliminary crystallographic studies of the hypothetical protein BPSL1038 from Burkholderia pseudomallei. Acta Crystallographica Section F:Structural Biology Communications, 70. pp. 1697-1700. ISSN 2053-230X 10.1107/S2053230X14025278
spellingShingle TP Chemical technology
Shaibullah, Sofiyah
Mohd-Sharif, Nurhikmah
Ho, Kok Lian
Raih, Mohd Firdaus
Nathan, Sheila
Rahmah, Mohamed
Ng, Chyan Leong
Crystallization and preliminary crystallographic studies of the hypothetical protein BPSL1038 from Burkholderia pseudomallei
title Crystallization and preliminary crystallographic studies of the hypothetical protein BPSL1038 from Burkholderia pseudomallei
title_full Crystallization and preliminary crystallographic studies of the hypothetical protein BPSL1038 from Burkholderia pseudomallei
title_fullStr Crystallization and preliminary crystallographic studies of the hypothetical protein BPSL1038 from Burkholderia pseudomallei
title_full_unstemmed Crystallization and preliminary crystallographic studies of the hypothetical protein BPSL1038 from Burkholderia pseudomallei
title_short Crystallization and preliminary crystallographic studies of the hypothetical protein BPSL1038 from Burkholderia pseudomallei
title_sort crystallization and preliminary crystallographic studies of the hypothetical protein bpsl1038 from burkholderia pseudomallei
topic TP Chemical technology
url http://eprints.intimal.edu.my/156/
http://eprints.intimal.edu.my/156/
http://eprints.intimal.edu.my/156/1/Crystallization%20and%20preliminary%20crystallographic%20studies%20of%20the%20hypothetical%20protein%20BPSL1038%20from%20Burkholderia%20pseudomallei.pdf