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 language | English |
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Journal | Acta Crystallographica Section D: Biological Crystallography |
Volume | 66 |
Issue | 3 |
Pages (from-to) | 309-313 |
Number of pages | 5 |
ISSN | 0907-4449 |
DOIs | |
Publication status | Published - 12 Feb 2010 |
Keywords
- Heavy-atom site identification
- Membrane proteins
- Molecular replacement
- Multi-crystal averaging