Reductive methylation to improve crystallization of the putative oxidoreductase Rv0765c from Mycobacterium tuberculosis
Journal Article
·
· Acta Crystallographica. Section F
- EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg (Germany)
- Max-Planck-Institute for Infection Biology, Schumannstrasse 21/22, D-10117 Berlin (Germany)
The M. tuberculosis protein Rv0765c was cloned, expressed, purified and crystallized. In an attempt to improve the quality of the crystals of Rv0765c, the protein was modified by reductive methylation. The methylated protein crystallized in a new crystal form with profoundly improved diffraction properties. Rv0765c from Mycobacterium tuberculosis was cloned and heterologously expressed in Escherichia coli. It was purified using affinity and size-exclusion chromatographic techniques and crystallized. The native protein crystallized in a hexagonal crystal form which diffracted to 7 Å resolution. In an attempt to improve the quality of the Rv0765c crystals, the protein was modified by reductive methylation using dimethylaminoborane and formaldehyde. The modified protein crystallized under different conditions in a tetragonal crystal form, from which diffraction data could be collected to a resolution of 3.2 Å. In both crystal forms of Rv0765c, the asymmetric unit contained two copies of the protein molecule.
- OSTI ID:
- 22360339
- Journal Information:
- Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 6 Vol. 63; ISSN ACSFCL; ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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