| Literature DB >> 10216317 |
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.Entities:
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Year: 1999 PMID: 10216317 DOI: 10.1107/s0907444999002875
Source DB: PubMed Journal: Acta Crystallogr D Biol Crystallogr ISSN: 0907-4449