| Literature DB >> 16754995 |
Christoph Thomas1, Michael Weyand, Alfred Wittinghofer, Antje Berken.
Abstract
The PRONE domain of the guanine nucleotide exchange factor RopGEF8 (PRONE8) was purified and crystallized free and in complex with the Rho-family protein Rop4 using the hanging-drop vapour-diffusion method. PRONE8 crystals were obtained using NaCl as precipitating agent and belong to the hexagonal space group P6(5)22. Native and anomalous data sets were collected using synchrotron radiation at 100 K to 2.2 and 2.8 A resolution, respectively. Crystals of the Rop4-PRONE8 complex belonging to space group P6(3) were obtained using Tacsimate and PEG 3350 as precipitating agents and diffracted to 3.1 A resolution.Entities:
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Year: 2006 PMID: 16754995 PMCID: PMC2243088 DOI: 10.1107/S1744309106018689
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091