English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Crystallization and preliminary X-ray structure analysis of thermally unstable p21H-ras guanosine complexes

Scheffzek, K., Kabsch, W., Schlichting, I., Pai, E. F., Lautwein, A., Frech, M., et al. (1994). Crystallization and preliminary X-ray structure analysis of thermally unstable p21H-ras guanosine complexes. Acta Crystallographica. Section D: Biological Crystallography (Copenhagen), 50(4), 521-526. doi:10.1107/S0907444994001253.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-A8FB-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-C280-0
Genre: Journal Article

Files

show Files
hide Files
:
ActaCrystD_50_1994_521.pdf (Any fulltext), 2MB
 
File Permalink:
-
Name:
ActaCrystD_50_1994_521.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-
Description:
-

Creators

show
hide
 Creators:
Scheffzek, Klaus1, Author              
Kabsch, Wolfgang2, Author              
Schlichting, Ilme3, Author              
Pai, Emil F., Author
Lautwein, Alfred, Author
Frech, Matthias, Author
Wittinghofer, Alfred, Author              
Goody, Roger S., Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
3Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753289              

Content

show
hide
Free keywords: -
 Abstract: p21 is a small guanine nucleotide binding protein that is involved in intracellular signal transduction. Biochemical data suggest that the presence of the [beta]-phosphate is essential for strong binding of guanine nucleotides to the protein. Guanosine or GMP bind six orders of magnitude more weakly to p21 than GDP or GTP. Moreover, the thermal stability of the protein is dramatically reduced when bound to GMP or guanosine. We have crystallized C-terminally truncated forms of p21H-ras, with guanosine or GMP bound, in the space groups P43212, P21212 and P21. The crystals diffract in the range 2.8-2.2 Å. Details of the crystallization procedures, the characterization of the crystals and preliminary results of structure determination are described. An unexpected electron-density peak was found close to the position of the [beta]-phosphate in the phosphate-binding loop.

Details

show
hide
Language(s): eng - English
 Dates: 1993-09-101994-01-311994-07-01
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 665165
DOI: 10.1107/S0907444994001253
Other: 6904
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Acta Crystallographica. Section D: Biological Crystallography (Copenhagen)
  Other : Acta Crystallogr D
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: [Copenhagen, Denmark : Published for the International Union of Crystallography by Munksgaard]
Pages: - Volume / Issue: 50 (4) Sequence Number: - Start / End Page: 521 - 526 Identifier: ISSN: 0907-4449
CoNE: https://pure.mpg.de/cone/journals/resource/954925562619