Crystallization and initial X-ray diffraction of BtuB, the integral membrane cobalamin transporter of Escherichia coli.

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Citation

Chimento DP, Mohanty AK, Kadner RJ, Wiener MC

Crystallization and initial X-ray diffraction of BtuB, the integral membrane cobalamin transporter of Escherichia coli.

Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):509-11. Epub 2003 Feb 21.

PubMed ID
12595710 [ View in PubMed
]
Abstract

BtuB, the cobalamin transporter from Escherichia coli, has been overexpressed, purified and crystallized. The purified protein was solubilized in n-octyl tetraoxyethylene (C(8)E(4)) and was crystallized using sitting-drop vapor diffusion with PEG 3350 and magnesium acetate as precipitants (pH 6.5). Two crystal forms have been obtained. Crystal type I belongs to space group P3(1)21, with unit-cell parameters a = b = 81.6, c = 210.0 A, alpha = beta = 90, gamma = 120 degrees. Crystal type II belongs to space group P3(1)21, with unit-cell parameters a = b = 81.6, c = 226.0 A, alpha = beta = 90, gamma = 120 degrees. Each crystal form contains a monomer in the asymmetric unit. Diffraction for crystal type I extends to 2.0 A and diffraction for crystal type II extends to 2.7 A. Both crystal forms are suitable for structure determination.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Vitamin B12 transporter BtuBP06129Details