Structure determination using poorly diffracting membrane-protein crystals: The H+-ATPase and Na+,K+-ATPase case history

Bjrn P. Pedersen, J. Preben Morth, Poul Nissen*

*Corresponding author for this work

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

13 Citations (Scopus)

Abstract

An approach is presented for the structure determination of membrane proteins on the basis of poorly diffracting crystals which exploits molecular replacement for heavy-atom site identification at 6-9 Å maximum resolution and improvement of the heavy-atom-derived phases by multi-crystal averaging using quasi-isomorphous data sets. The multi-crystal averaging procedure allows real-space density averaging followed by phase combination between non-isomorphous native data sets to exploit crystal-to-crystal nonisomorphism despite the crystals belonging to the same space group. This approach has been used in the structure determination of H+-ATPase and Na +,K+-ATPase using Ca2+-ATPase models and its successful application to the Mhp1 symporter using LeuT as a search model is demonstrated.

Original languageEnglish
JournalActa Crystallographica Section D: Biological Crystallography
Volume66
Issue3
Pages (from-to)309-313
Number of pages5
ISSN0907-4449
DOIs
Publication statusPublished - 12 Feb 2010

Keywords

  • Heavy-atom site identification
  • Membrane proteins
  • Molecular replacement
  • Multi-crystal averaging

Fingerprint

Dive into the research topics of 'Structure determination using poorly diffracting membrane-protein crystals: The H+-ATPase and Na+,K+-ATPase case history'. Together they form a unique fingerprint.

Cite this