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

Gorynia, S.; Matias, P.M.; Gonçalves, S.; Coelho, R.; Lopes, G.; Thomaz, M.; Huber, M.; Haendler, B.; Donner, P.; Carrondo, M.A.

doi:10.1107/S1744309105041400

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

S. Gorynia, P. M. Matias, S. Gonçalves, R. Coelho, G. Lopes, M. Thomaz, M. Huber, B. Haendler, P. Donner and M. A. Carrondo

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 Å and three molecules in the asymmetric unit.

Keywords: RuvBL1.

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

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