Protein crystal screening and characterization for serial femtosecond nanocrystallography

被引：25
作者：
Darmanin, Connie [1 ]
Strachan, Jamie [1 ]
Adda, Christopher G. [2 ]
Ve, Thomas [3 ,4 ,5 ,6 ]
Kobe, Bostjan [3 ,4 ,5 ]
Abbey, Brian [1 ,7 ]
机构：
[1] La Trobe Univ, La Trobe Inst Mol Sci, Dept Chem & Phys, ARC Ctr Adv Mol Imaging, Melbourne, Vic 3086, Australia
[2] La Trobe Univ, La Trobe Inst Mol Sci, Dept Biochem & Genet, Melbourne, Vic 3086, Australia
[3] Univ Queensland, Sch Chem & Mol Biosci, Brisbane, Qld 4072, Australia
[4] Univ Queensland, Inst Mol Biosci, Div Chem & Struct Biol, Brisbane, Qld 4072, Australia
[5] Univ Queensland, Australian Infect Dis Res Ctr, Brisbane, Qld 4072, Australia
[6] Griffith Univ, Inst Glyc, Gold Coast Campus, Southport, Qld 4222, Australia
[7] Melbourne Ctr Nanofabricat, Melbourne, Vic 3168, Australia
来源：
SCIENTIFIC REPORTS | 2016年 / 6卷
基金：
英国医学研究理事会;
关键词：
CRYSTALLOGRAPHY; CRYSTALLIZATION; RHODOPSIN;
D O I：
10.1038/srep25345
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
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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页数：8
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