Open AccessPurification and crystallization of the catalytic PRONE domain of RopGEF8 and its complex with Rop4 from Arabidopsis thaliana
Author(s) -
Thomas Christoph,
Weyand Michael,
Wittinghofer Alfred,
Berken Antje
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106018689
Subject(s) - crystallization , guanine nucleotide exchange factor , crystallography , synchrotron radiation , arabidopsis thaliana , drop (telecommunication) , resolution (logic) , chemistry , nucleotide , peg ratio , materials science , gtpase , biochemistry , physics , organic chemistry , optics , gene , mutant , telecommunications , finance , artificial intelligence , computer science , economics
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 P 6 5 22. Native and anomalous data sets were collected using synchrotron radiation at 100 K to 2.2 and 2.8 Å resolution, respectively. Crystals of the Rop4–PRONE8 complex belonging to space group P 6 3 were obtained using Tacsimate and PEG 3350 as precipitating agents and diffracted to 3.1 Å resolution.