Abstract：
:Serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs) is a powerful method to determine high-resolution structures of pharmaceutically relevant membrane proteins. Recently, the technology has been adapted to carry out serial millisecond crystallography (SMX) at synchrotron sources, where beamtime is more abundant. In an injector-based approach, crystals grown in lipidic cubic phase (LCP) or embedded in viscous medium are delivered directly into the unattenuated beam of a microfocus beamline. Pilot experiments show the application of microjet-based SMX for solving the structure of a membrane protein and compatibility of the method with de novo phasing. Planned synchrotron upgrades, faster detectors and software developments will go hand-in-hand with developments at free-electron lasers to provide a powerful methodology for solving structures from microcrystals at room temperature, ligand screening or crystal optimization for time-resolved studies with minimal or no radiation damage.
journal_name
Adv Exp Med Bioljournal_title
Advances in experimental medicine and biologyauthors
Jaeger K,Dworkowski F,Nogly P,Milne C,Wang M,Standfuss Jdoi
10.1007/978-3-319-35072-1_10subject
Has Abstractpub_date
2016-01-01 00:00:00pages
137-149eissn
0065-2598issn
2214-8019journal_volume
922pub_type
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