The purification and crystallization of mDia1 in complex with RhoC

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Rolf RoseMichael Weyand

Abstract

An N-terminal construct of mouse mDia1 was recombinantly expressed in Escherichia coli, purified and crystallized in complex with truncated human RhoC using the hanging-drop vapour-diffusion method. Crystals were obtained using PEG 2K MME and MgSO4 as a precipitating agent and belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 148.4, b = 85.2, c = 123.2 A. Complete native and SeMet-derivative data sets were collected at 100 K to 3.0 and 3.4 A resolution, respectively, using synchrotron radiation.

References

Apr 28, 1968·Journal of Molecular Biology·B W Matthews
Nov 10, 2001·Science·I R Vetter, A Wittinghofer
Jul 4, 2002·Methods in Molecular Biology·Mohammad Reza AhmadianChristian Herrmann
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Citations

Jan 12, 2010·Nature Structural & Molecular Biology·Masami YamashitaShuya Fukai
Oct 3, 2008·The Journal of Biological Chemistry·Michael LammersAlfred Wittinghofer
Nov 18, 2005·The EMBO Journal·Michael LammersAlfred Wittinghofer
Sep 22, 2021·Proceedings of the National Academy of Sciences of the United States of America·Sergio G BartualDaan M F van Aalten

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