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.
Links
MeSH
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 -