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Mark S. Hunter

Researcher at SLAC National Accelerator Laboratory

Publications -  120
Citations -  10007

Mark S. Hunter is an academic researcher from SLAC National Accelerator Laboratory. The author has contributed to research in topics: Femtosecond & Laser. The author has an hindex of 39, co-authored 104 publications receiving 8681 citations. Previous affiliations of Mark S. Hunter include Lawrence Livermore National Laboratory & Arizona State University.

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Femtosecond X-ray protein nanocrystallography

Henry N. Chapman, +88 more
- 03 Feb 2011 - 
TL;DR: This work offers a new approach to structure determination of macromolecules that do not yield crystals of sufficient size for studies using conventional radiation sources or are particularly sensitive to radiation damage, by using pulses briefer than the timescale of most damage processes.
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Single mimivirus particles intercepted and imaged with an X-ray laser

M. Marvin Seibert, +88 more
- 03 Feb 2011 - 
TL;DR: This work shows that high-quality diffraction data can be obtained with a single X-ray pulse from a non-crystalline biological sample, a single mimivirus particle, which was injected into the pulsed beam of a hard-X-ray free-electron laser, the Linac Coherent Light Source.
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High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography

TL;DR: Serial femtosecond crystallography (SFX) is applied using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals of the well-characterized model protein lysozyme, demonstrating the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.
Journal ArticleDOI

Serial time-resolved crystallography of photosystem II using a femtosecond X-ray laser.

TL;DR: Time resolved experiments on PSII nano/microcrystals from Thermosynechococcus elongatus performed with the recently developed technique of serial femtosecond crystallography provide evidence that PSII undergoes significant conformational changes at the electron acceptor side and at the Mn4CaO5 core of the OEC.