Volume 55, Issue 7 pp. 1356-1358

Crystallization and preliminary X-ray studies on the molbindin ModG from Azotobacter vinelandii

Clare E. M. Williams

Clare E. M. Williams

Nitrogen Fixation Laboratory, John Innes Centre, Norwich NR4 7UH, England

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Daniel J. White

Daniel J. White

Nitrogen Fixation Laboratory, John Innes Centre, Norwich NR4 7UH, England

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Laure Delarbre

Laure Delarbre

Nitrogen Fixation Laboratory, John Innes Centre, Norwich NR4 7UH, England

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Lesley A. Mitchenall

Lesley A. Mitchenall

Nitrogen Fixation Laboratory, John Innes Centre, Norwich NR4 7UH, England

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Richard N. Pau

Richard N. Pau

Nitrogen Fixation Laboratory, John Innes Centre, Norwich NR4 7UH, England

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David M. Lawson

David M. Lawson

Nitrogen Fixation Laboratory, John Innes Centre, Norwich NR4 7UH, England

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First published: 27 September 2007

Abstract

Crystals of the molbindin ModG (subunit Mr = 14359 Da), a cytoplasmic molybdate-binding protein from Azotobacter vinelandii, were grown by vapour diffusion. Both apo and tungstate-bound forms were crystallized and X-ray data were collected at 100 K. Apo-ModG crystallizes in space group P6322, with unit-cell dimensions a = b = 90.62, c = 79.46 Å. Native data to a resolution of 2.5 Å were collected from a single crystal, which showed a marked improvement in diffraction quality after annealing. Data from a single-site gold derivative were also collected at 2.7 Å resolution. Crystals of the ligand-bound form of ModG belong to space group P321, with unit-cell parameters a = b = 50.57, c = 79.29 Å. X-ray data to a resolution of 2.0 Å were collected.

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