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PLoS One. 2009 Jun 2;4(6):e5769. doi: 10.1371/journal.pone.0005769.

Protein conformational changes in the bacteriorhodopsin photocycle: comparison of findings from electron and X-ray crystallographic analyses.

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  • 1Laboratory of Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, USA.

Erratum in

  • PLoS One. 2009;4(6). doi: 10.1371/annotation/dab20871-1ee8-473c-92b0-2a4550b4b09a.
  • PLoS One. 2009;4(7). doi: 10.1371/annotation/b7d18825-44b9-4ff1-9478-321049172908.
  • PLoS One. 2009;4(7). doi: 10.1371/annotation/dab20871-1ee8-473c-92b0-2a4550b4b09a.
  • PLoS One. 2009;4(6). doi: 10.1371/annotation/b7d18825-44b9-4ff1-9478-321049172908.


Light-driven conformational changes in the membrane protein bacteriorhodopsin have been studied extensively using X-ray and electron crystallography, resulting in the deposition of >30 sets of coordinates describing structural changes at various stages of proton transport. Using projection difference Fourier maps, we show that coordinates reported by different groups for the same photocycle intermediates vary considerably in the extent and nature of conformational changes. The different structures reported for the same intermediate cannot be reconciled in terms of differing extents of change on a single conformational trajectory. New measurements of image phases obtained by cryo-electron microscopy of the D96G/F171C/F219L triple mutant provide independent validation for the description of the large protein conformational change derived at 3.2 A resolution by electron crystallography of 2D crystals, but do not support atomic models for light-driven conformational changes derived using X-ray crystallography of 3D crystals. Our findings suggest that independent determination of phase information from 2D crystals can be an important tool for testing the accuracy of atomic models for membrane protein conformational changes.

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