Saikrishnan, K and Jeyakanthan, J and Venkatesh, J and Acharya, N and Purnapatre, K and Sekar, K and Varshney, U and Vijayan, M (2002) Crystallization and preliminary X-ray studies of the single-stranded DNA-binding protein from Mycobacterium tuberculosis. In: Acta Crystallographica Section D, 58 . pp. 327-329.
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Single-stranded DNA-binding proteins play an important role in DNA replication, repair and recombination. The protein from Mycobacterium tuberculosis (MtSSB) is a tetramer with 164 aminoacid residues in each subunit. The protein readily crystallizes in space group P3121 (or P3221) at pH 7.4 under appropriate conditions. Under different conditions, but at the same pH, orthorhombic crystals belonging to space group I222 or I212121 were obtained after several months. Similar orthorhombic crystals were obtained when protein samples stored for several months were used for crystallization. The orthorhombic crystals obtained in different experiments, though similar to one another, exhibited variations in unit-cell parameters, presumably on account of different extents of proteolytic cleavage of the C-terminal region. Molecular-replacement calculations using different search models did not yield the structure. As part of attempts to solve the structure using isomorphous replacement, a good mercury derivative of the trigonal crystal has been prepared.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to International Union of Crystallography.|
|Keywords:||dna binding,crystallization;x ray studies;protein; mycobacterium tuberculosis;orthorhombic crystals|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit
Division of Information Sciences > BioInformatics Centre
Division of Biological Sciences > Microbiology & Cell Biology
|Date Deposited:||12 Oct 2004|
|Last Modified:||23 Feb 2012 09:28|
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