Journal
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES
Volume 369, Issue 1647, Pages -Publisher
ROYAL SOC
DOI: 10.1098/rstb.2013.0500
Keywords
two-dimensional protein crystal; X-ray diffraction; X-ray free-electron laser; crystallographic data analysis; bacteriorhodopsin
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Funding
- US Department of Energy by Lawrence Livermore National Laboratory [DE-AC52-07NA27344]
- Pacific Northwest National Laboratory [DE-AC05-76RL01830]
- UCOP Lab Fee Programme [118036]
- NIH [5RC1GM091755, GM095583]
- NSF [MCB-1021557]
- NSF STC [1231306]
- LLNL Lab-Directed Research and Development Project [012-ERD-031]
- PNNL Chemical Imaging Initiative
- Center for Biophotonics Science and Technology, a designated NSF Science and Technology Center [PHY0120999]
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Membrane proteins arranged as two-dimensional crystals in the lipid environment provide close-to-physiological structural information, which is essential for understanding the molecular mechanisms of protein function. Previously, X-ray diffraction from individual two-dimensional crystals did not represent a suitable investigational tool because of radiation damage. The recent availability of ultrashort pulses from X-ray free-electron lasers (XFELs) has now provided a means to outrun the damage. Here, we report on measurements performed at the Linac Coherent Light Source XFEL on bacteriorhodopsin two-dimensional crystals mounted on a solid support and kept at room temperature. By merging data from about a dozen single crystal diffraction images, we unambiguously identified the diffraction peaks to a resolution of 7 angstrom, thus improving the observable resolution with respect to that achievable from a single pattern alone. This indicates that a larger dataset will allow for reliable quantification of peak intensities, and in turn a corresponding increase in the resolution. The presented results pave the way for further XFEL studies on two-dimensional crystals, which may include pump-probe experiments at subpicosecond time resolution.
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