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In situ serial Laue diffraction on a microfluidic crystallization device.


ABSTRACT: 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.

SUBMITTER: Perry SL 

PROVIDER: S-EPMC4248567 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature

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<i>In situ</i> serial Laue diffraction on a microfluidic crystallization device.

Perry Sarah L SL   Guha Sudipto S   Pawate Ashtamurthy S AS   Henning Robert R   Kosheleva Irina I   Srajer Vukica V   Kenis Paul J A PJ   Ren Zhong Z  

Journal of applied crystallography 20141118 Pt 6


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  ...[more]

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