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Expression, purification, crystallization and preliminary X-ray analysis of the human RuvB-like protein RuvBL1.

ABSTRACT: RuvBL1, an evolutionary highly conserved protein related to the AAA+ family of ATPases, has been crystallized using the hanging-drop vapour-diffusion method at 293 K. The crystals are hexagonal and belong to space group P6, with unit-cell parameters a = b = 207.1, c = 60.7 A and three molecules in the asymmetric unit.

SUBMITTER: Gorynia S

PROVIDER: S-EPMC2150925 | biostudies-literature | 2006 Jan

REPOSITORIES: biostudies-literature

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Expression, purification, crystallization and preliminary X-ray analysis of the human RuvB-like protein RuvBL1.

Gorynia Sabine S Matias Pedro M PM Gonçalves Susana S Coelho Ricardo R Lopes Gonçalo G Thomaz Mónica M Huber Martina M Haendler Bernard B Donner Peter P Carrondo Maria Arménia MA

Acta crystallographica. Section F, Structural biology and crystallization communications 20051216 Pt 1

RuvBL1, an evolutionary highly conserved protein related to the AAA+ family of ATPases, has been crystallized using the hanging-drop vapour-diffusion method at 293 K. The crystals are hexagonal and belong to space group P6, with unit-cell parameters a = b = 207.1, c = 60.7 A and three molecules in the asymmetric unit. ...[more]

PMID: 16511264

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