Electron Crystallography of Bacteriorhodopsin with Millisecond Time Resolution
Journal of Structural Biology, ISSN: 1047-8477, Vol: 128, Issue: 1, Page: 19-25
1999
- 43Citations
- 54Captures
Metric Options: Counts1 Year3 YearSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations43
- Citation Indexes43
- 43
- CrossRef40
- Captures54
- Readers54
- 54
Article Description
The goal of time-resolved crystallographic experiments is to capture dynamic “snapshots” of molecules at different stages of a reaction pathway. In recent work, we have developed approaches to determine determined light-induced conformational changes in the proton pump bacteriorhodopsin by electron crystallographic analysis of two-dimensional protein crystals. For this purpose, crystals of bacteriorhodopsin were deposited on an electron microscopic grid and were plunge-frozen in liquid ethane at a variety of times after illumination. Electron diffraction patterns were recorded either from unilluminated crystals or from crystals frozen as early as 1 ms after illumination and used to construct projection difference Fourier maps at 3.5-Å resolution to define light-driven changes in protein conformation. As demonstrated here, the data are of a sufficiently high quality that structure factors obtained from a single electron diffraction pattern of a plunge-frozen bacteriorhodopsin crystal are adequate to obtain an interpretable difference Fourier map. These difference maps report on the nature and extent of light-induced conformational changes in the photocycle and have provided incisive tools for understanding the molecular mechanism of proton transport by bacteriorhodopsin.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S1047847799941783; http://dx.doi.org/10.1006/jsbi.1999.4178; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0033386253&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/10600554; https://linkinghub.elsevier.com/retrieve/pii/S1047847799941783; https://dx.doi.org/10.1006/jsbi.1999.4178
Elsevier BV
Provide Feedback
Have ideas for a new metric? Would you like to see something else here?Let us know