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Gorynia, S. et al.

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

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.[1]

References

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. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2006) [Pubmed]

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