In situserial Laue diffraction on a microfluidic crystallization device
2014 ◽
Vol 47
(6)
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pp. 1975-1982
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Keyword(s):
X Ray
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Renewed interest in room-temperature diffraction has been prompted by the desire to observe structural dynamics of proteins as they function. Serial crystallography, an experimental strategy that aggregates small pieces of data from a large uniform pool of crystals, has been demonstrated at synchrotrons and X-ray free-electron lasers. This work utilizes a microfluidic crystallization platform for serial Laue diffraction from macroscopic crystals and proposes that a collection of small slices of Laue data from many individual crystals is a realistic solution to the difficulties in dynamic studies of irreversible biochemical reactions.
2019 ◽
Vol 88
(1)
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pp. 35-58
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2014 ◽
Vol 369
(1647)
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pp. 20130337
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2015 ◽
Vol 86
(9)
◽
pp. 093104
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2015 ◽
Vol 71
(2)
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pp. 352-356
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