Literature DB >> 10216317

Crystallization and preliminary X-ray diffraction studies of bleomycin-binding protein encoded on the transposon Tn5.

T Kumagai1, M Maruyama, Y Matoba, Y Kawano, M Sugiyama.   

Abstract

A bleomycin-binding protein, designated BLMT, encoded on the transposon Tn5 was crystallized using the vapour-diffusion method in a form suitable for X-ray diffraction analysis. Crystals were grown at pH 6.5 in 0.1 M sodium cacodylate and 0.2 M calcium acetate, using 25% PEG 6000 as a precipitant. They belong to the orthorhombic system, space group C2221, with unit-cell dimensions a = 81.56, b = 85.25, c = 78.91 A and one dimer in the asymmetric unit. The diffraction intensity data were collected on beamline 18B of the Photon Factory to 2.0 A resolution with a merging R value of 0.052. The diffraction data set is 91% complete.

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Year:  1999        PMID: 10216317     DOI: 10.1107/s0907444999002875

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


  2 in total

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Authors:  Masanori Sugiyama
Journal:  J Antibiot (Tokyo)       Date:  2015-04-15       Impact factor: 2.649

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Authors:  I Mulako; J M Farrant; H Collett; N Illing
Journal:  J Exp Bot       Date:  2008-09-12       Impact factor: 6.992

  2 in total

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