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Cloning, overexpression, purification, crystallization and preliminary X-ray studies of SP-0149, the substrate binding protein of an ABC transporter from Streptococcus pneumoniae
Jaya Bhushan, , Tripti Sharma, Devinder Sehgal, Bichitra Biswal Kumar
Published in
Volume: 67
Issue: 7
Pages: 797 - 799
A truncated (29 residues from the N-terminus) and N-terminal His-tagged form of SP-0149 from pneumococcal strain ATCC BAA-334 was overexpressed and purified to homogeneity using affinity and gel-filtration chromatography. Diffraction quality crystals were grown at 293 K using the hanging-drop vapour-diffusion technique. X-ray diffraction data were collected to 2.3 {\AA} resolution from a single-crystal that belonged to the orthorhombic space group P2 12 12 1 with the unit-cell parameters a = 54.56, b = 75.61, c = 75.52 {\AA}. The calculated values of the Matthews coefficient assuming one molecule (with calculated molecular weight of 30 400 Da) in the crystal asymmetric unit and the corresponding solvent content were 2.56 {\AA} 3 Da -1 and 52.0%, respectively. {\textcopyright} 2011 International Union of Crystallography All rights reserved.
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