Special Issue "Protein Crystallography 2016"
A special issue of Biomolecules (ISSN 2218-273X).
Deadline for manuscript submissions: closed (30 June 2017)
We are interested in the use of radiation from the X-ray free electron laser (XFEL) for protein structure determination. An XFEL is capable of producing X-rays that are ten billion (1010) times brighter that any previous X-ray source. When one considers that protein crystallography is usually done on samples containing perhaps a trillion (1012) molecules, an intriguing question is whether the extra brightness of the XFEL will allow structure determination from individual molecules. One has to be content with signals, which are perhaps a hundred times smaller. Of course, a single molecule will scatter only diffuse intensities, devoid of Bragg spots. Finally, sample delivery systems probably will not be able to control the orientations of the samples, which should perhaps be regarded as randomly oriented.
Despite these differences with traditional protein crystallography, if structure determination is possible, it would allow structure determination of even uncrystallized proteins. This is important because there exist entire classes of proteins, e.g., membrane proteins, which are very resistant to crystallization.
Prof. Dr. Dilano K. Saldin
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- membrane protein structure
- weak signals
- unknown orientations