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  Crystallographic studies on p21H-ras using the synchrotron Laue method: improvement of crystal quality and monitoring of the GTPase reaction at different time points

Scheidig, A. J., Sanchez-Llorente, A., Lautwein, A., Pai, E. F., Corrie, J. E. T., Reid, G. P., et al. (1994). Crystallographic studies on p21H-ras using the synchrotron Laue method: improvement of crystal quality and monitoring of the GTPase reaction at different time points. Acta Crystallographica. Section D: Biological Crystallography (Copenhagen), 50(4), 512-520. doi:10.1107/S090744499301443X.

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Datensatz-Permalink: https://hdl.handle.net/11858/00-001M-0000-0019-A961-8 Versions-Permalink: https://hdl.handle.net/11858/00-001M-0000-002D-C282-C
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 Urheber:
Scheidig, Axel J.1, Autor           
Sanchez-Llorente, Antonieta1, Autor           
Lautwein, Alfred1, Autor           
Pai, Emil F., Autor
Corrie, John E. T., Autor
Reid, Gordon P., Autor
Wittinghofer, Alfred1, Autor           
Goody, Roger S.1, Autor           
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Zusammenfassung: The parameters affecting the crystal quality of complexes between p21H-ras and caged GTP have been investigated. The use of pure diastereomers of caged GTP complexed to the more stable p21(G12P)' mutant of p21 and the addition of n-octyl-[beta]-D-glucopyranoside improved the reproducibility and decreased the mosaicity of the crystals significantly. Furthermore, the crystallization technique was changed from the batch method to the sitting-drop technique. With the availability of a larger yield of well ordered crystals, it was possible to extend the time-resolved crystallographic investigations on p21H-ras. A structure of p21(G12P)':GTP could be obtained 2 min after photolytic removal of the cage group and led to the identification of a previously unidentified conformation for the so-called catalytically active loop L4. The refinement of five data sets collected within 2 min at different times (2-4, 11-13, 20-22, 30-32 and 90-92 min) after the initiation of the intrinsic GTPase reaction of the protein indicates that the synchrotron Laue method can be used to detect small structural changes and alternative conformations, but is presently limited in the analysis of larger rearrangements since these produce diffuse and broken electron density.

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Sprache(n): eng - English
 Datum: 1993-09-101993-12-221994
 Publikationsstatus: Erschienen
 Seiten: 9
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 665162
DOI: 10.1107/S090744499301443X
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Titel: Acta Crystallographica. Section D: Biological Crystallography (Copenhagen)
  Alternativer Titel : Acta Crystallogr. Sec. D
Genre der Quelle: Zeitschrift
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Affiliations:
Ort, Verlag, Ausgabe: [Copenhagen, Denmark : Published for the International Union of Crystallography by Munksgaard]
Seiten: - Band / Heft: 50 (4) Artikelnummer: - Start- / Endseite: 512 - 520 Identifikator: ISSN: 0907-4449