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. 2010 Mar;66(Pt 3):309-13.
doi: 10.1107/S0907444909053244. Epub 2010 Feb 12.

Structure Determination Using Poorly Diffracting Membrane-Protein Crystals: The H+-ATPase and Na+,K+-ATPase Case History

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Structure Determination Using Poorly Diffracting Membrane-Protein Crystals: The H+-ATPase and Na+,K+-ATPase Case History

Bjørn P Pedersen et al. Acta Crystallogr D Biol Crystallogr. .

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 A 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 Ca(2+)-ATPase models and its successful application to the Mhp1 symporter using LeuT as a search model is demonstrated.

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