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Purification, crystallization and preliminary structural characterization of human Rap1GAP.
Acta Crystallogr D Biol Crystallogr. 2004 Apr; 60(Pt 4):752-4.AC

Abstract

Human Rap1GAP, the GTPase-activating protein (GAP) for the small GTPase Rap1, was recombinantly expressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. Crystals were obtained using PEG 3350 as a precipitating agent and belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 170.7, b = 224.5, c = 48.7 A. A complete data set was collected to 2.9 A resolution at 100 K using synchrotron radiation. The structure may reveal features of the unique reaction mechanism of Rap1GAP.

Authors+Show Affiliations

Max-Planck-Institute für Molekulare Physiologie, Abteilung Strukturbiologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15039575

Citation

Daumke, Oliver, et al. "Purification, Crystallization and Preliminary Structural Characterization of Human Rap1GAP." Acta Crystallographica. Section D, Biological Crystallography, vol. 60, no. Pt 4, 2004, pp. 752-4.
Daumke O, Wittinghofer A, Weyand M. Purification, crystallization and preliminary structural characterization of human Rap1GAP. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 4):752-4.
Daumke, O., Wittinghofer, A., & Weyand, M. (2004). Purification, crystallization and preliminary structural characterization of human Rap1GAP. Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 4), 752-4.
Daumke O, Wittinghofer A, Weyand M. Purification, Crystallization and Preliminary Structural Characterization of Human Rap1GAP. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 4):752-4. PubMed PMID: 15039575.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification, crystallization and preliminary structural characterization of human Rap1GAP. AU - Daumke,Oliver, AU - Wittinghofer,Alfred, AU - Weyand,Michael, Y1 - 2004/03/23/ PY - 2004/01/20/received PY - 2004/01/29/accepted PY - 2004/3/25/pubmed PY - 2004/12/16/medline PY - 2004/3/25/entrez SP - 752 EP - 4 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 4 N2 - Human Rap1GAP, the GTPase-activating protein (GAP) for the small GTPase Rap1, was recombinantly expressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. Crystals were obtained using PEG 3350 as a precipitating agent and belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 170.7, b = 224.5, c = 48.7 A. A complete data set was collected to 2.9 A resolution at 100 K using synchrotron radiation. The structure may reveal features of the unique reaction mechanism of Rap1GAP. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/15039575/Purification_crystallization_and_preliminary_structural_characterization_of_human_Rap1GAP_ DB - PRIME DP - Unbound Medicine ER -