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

• 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
• Subjects: TP Chemical technology
• Online Access: http://eprints.intimal.edu.my/156/1/Crystallization%20and%20preliminary%20crystallographic%20studies%20of%20the%20hypothetical%20protein%20BPSL1038%20from%20Burkholderia%20pseudomallei.pdf; http://eprints.intimal.edu.my/156/

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%.