Literature DB >> 11053850

Crystallization and preliminary X-ray diffraction studies on the DNA-binding domain of the multidrug transporter activation protein (MtaN) from Bacillus subtilis.

M H Godsey1, N N Baranova, A A Neyfakh, R G Brennan.   

Abstract

The N-terminal DNA-binding domain of the multidrug transporter activation protein (MtaN) was crystallized by the hanging-drop vapour-diffusion method using lithium chloride as a precipitant. The crystals are orthorhombic and belong to the space group I2(1)2(1)2(1), with unit-cell parameters a = 49.4, b = 67.8, c = 115. 0 A. Diffraction data have been collected at 100 K to 2.75 A resolution at a synchrotron-radiation source.

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Year:  2000        PMID: 11053850     DOI: 10.1107/s0907444900010295

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  1 in total

1.  The major facilitator superfamily-type transporter YmfE and the multidrug-efflux activator Mta mediate bacillibactin secretion in Bacillus subtilis.

Authors:  Marcus Miethke; Sarah Schmidt; Mohamed A Marahiel
Journal:  J Bacteriol       Date:  2008-05-23       Impact factor: 3.490

  1 in total

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