Whole-pattern fitting technique in serial femtosecond nanocrystallography.

ABSTRACT: Serial femtosecond X-ray crystallography (SFX) has created new opportunities in the field of structural analysis of protein nanocrystals. The intensity and timescale characteristics of the X-ray free-electron laser sources used in SFX experiments necessitate the analysis of a large collection of individual crystals of variable shape and quality to ultimately solve a single, average crystal structure. Ensembles of crystals are commonly encountered in powder diffraction, but serial crystallography is different because each crystal is measured individually and can be oriented via indexing and merged into a three-dimensional data set, as is done for conventional crystallography data. In this way, serial femtosecond crystallography data lie in between conventional crystallography data and powde

SUBMITTER: Dilanian RA 

PROVIDER: S-EPMC4775161 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature