Cargando…

Protein crystal screening and characterization for serial femtosecond nanocrystallography

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 us...

Descripción completa

Detalles Bibliográficos
Autores principales: Darmanin, Connie, Strachan, Jamie, Adda, Christopher G., Ve, Thomas, Kobe, Bostjan, Abbey, Brian
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4853777/
https://www.ncbi.nlm.nih.gov/pubmed/27139248
http://dx.doi.org/10.1038/srep25345
Descripción
Sumario: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.