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

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Sabine GoryniaMaria Arménia Carrondo

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.

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Citations

Jan 1, 2012·Rice·Chai-Ling HoMatt Geisler
Oct 25, 2006·The Journal of Biological Chemistry·Pedro M MatiasMaria Arménia Carrondo

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