Protein crystal screening and characterization for serial femtosecond nanocrystallography

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作者
Connie Darmanin
Jamie Strachan
Christopher G. Adda
Thomas Ve
Bostjan Kobe
Brian Abbey
机构
[1] ARC Centre of Advanced Molecular Imaging,Department of Chemistry and Physics
[2] La Trobe Institute for Molecular Science,Department of Biochemistry and Genetics
[3] La Trobe University,School of Chemistry and Molecular Biosciences and Institute for Molecular Bioscience (Division of Chemistry and Structural Biology) and Australian Infectious Diseases Research Centre
[4] La Trobe Institute for Molecular Science,undefined
[5] La Trobe University,undefined
[6] University of Queensland,undefined
[7] Institute for Glycomics,undefined
[8] Griffith University,undefined
[9] Gold Coast Campus,undefined
[10] Melbourne Centre for Nanofabrication,undefined
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摘要
The recent development of X-ray free electron lasers (XFELs) has spurred the development of serial femtosecond nanocrystallography (SFX) which, for the first time, is enabling structure retrieval from sub-micron protein crystals. Although there are already a growing number of structures published using SFX, the technology is still very new and presents a number of unique challenges as well as opportunities for structural biologists. One of the biggest barriers to the success of SFX experiments is the preparation and selection of suitable protein crystal samples. Here we outline a protocol for preparing and screening for suitable XFEL targets.
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