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The purification and crystallization of mDia1 in complex with RhoC.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Feb 01; 61(Pt 2):225-7.AC

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.

Authors+Show Affiliations

Department of Structural Biology, Max-Planck-Institut für Molekulare Physiologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

16511001

Citation

Rose, Rolf, et al. "The Purification and Crystallization of mDia1 in Complex With RhoC." Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, vol. 61, no. Pt 2, 2005, pp. 225-7.
Rose R, Wittinghofer A, Weyand M. The purification and crystallization of mDia1 in complex with RhoC. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005;61(Pt 2):225-7.
Rose, R., Wittinghofer, A., & Weyand, M. (2005). The purification and crystallization of mDia1 in complex with RhoC. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, 61(Pt 2), 225-7.
Rose R, Wittinghofer A, Weyand M. The Purification and Crystallization of mDia1 in Complex With RhoC. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Feb 1;61(Pt 2):225-7. PubMed PMID: 16511001.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The purification and crystallization of mDia1 in complex with RhoC. AU - Rose,Rolf, AU - Wittinghofer,Alfred, AU - Weyand,Michael, Y1 - 2005/02/01/ PY - 2004/12/22/received PY - 2005/01/11/accepted PY - 2006/3/3/pubmed PY - 2006/5/16/medline PY - 2006/3/3/entrez SP - 225 EP - 7 JF - Acta crystallographica. Section F, Structural biology and crystallization communications JO - Acta Crystallogr Sect F Struct Biol Cryst Commun VL - 61 IS - Pt 2 N2 - 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. SN - 1744-3091 UR - https://www.unboundmedicine.com/medline/citation/16511001/The_purification_and_crystallization_of_mDia1_in_complex_with_RhoC_ DB - PRIME DP - Unbound Medicine ER -