PlumX Metrics
Embed PlumX Metrics

The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: implication of the charge distribution 1 1Edited by R. Huber

Journal of Molecular Biology, ISSN: 0022-2836, Vol: 286, Issue: 3, Page: 861-882
1999
  • 241
    Citations
  • 0
    Usage
  • 95
    Captures
  • 0
    Mentions
  • 0
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

Article Description

Electron crystallography has the potential to visualise the charge status of atoms. This is due to the significantly different scattering factors of neutral and ionised atoms for electrons in the low-resolution range (typically less than 5 Å). In previous work, we observed two different types of densities around acidic residues in the experimental (| F o |) map of bacteriorhodopsin (bR), a light-driven proton pump. We suggested that these might reflect different states of the acidic residues; namely, the protonated (neutral) and the deprotonated (negatively charged) state. To evaluate the observed charge more quantitatively, we refined the atomic model for bR and eight surrounding lipids using our electron crystallographic data set between 8.0 and 3.0 Å resolution, where the charge effect is small. The refined model yielded an R -factor of 23.7 % and a free R -factor of 33.0 %.

Bibliographic Details

Provide Feedback

Have ideas for a new metric? Would you like to see something else here?Let us know