title: Reductive methylation to improve crystallization of the putative oxidoreductase Rv0765c from Mycobacterium tuberculosis.
abstract: 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 A 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 A. In both crystal forms of Rv0765c, the asymmetric unit contained two copies of the protein molecule.
authors.affiliation: EMBL Hamburg Outstation, DESY, Hamburg, Germany.
authors.forename: Wilko
authors.initials: W
authors.lastname: Rauert
authors.forename: Ali Nasser
authors.initials: AN
authors.lastname: Eddine
authors.forename: Stefan H E
authors.initials: SH
authors.lastname: Kaufmann
authors.forename: Manfred S
authors.initials: MS
authors.lastname: Weiss
authors.forename: Robert
authors.initials: R
authors.lastname: Janowski
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001880:Boranes / Q000737:chemistry / Q000378:metabolism; D003460:Crystallization; D005557:Formaldehyde / Q000737:chemistry / Q000378:metabolism; D008745:Methylation; D009169:Mycobacterium tuberculosis / Q000737:chemistry* / Q000201:enzymology*; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry* / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D001880:Boranes; D005557:Formaldehyde; D010088:Oxidoreductases