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 af dette arbejde

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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.

OriginalsprogEngelsk
TidsskriftActa Crystallographica Section D: Biological Crystallography
Vol/bind66
Nummer3
Sider (fra-til)309-313
Antal sider5
ISSN0907-4449
DOI
StatusUdgivet - 12 feb. 2010

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