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2016 ; 3
(Pt 2
): 127-38
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Whole-pattern fitting technique in serial femtosecond nanocrystallography
#MMPMID27006776
Dilanian RA
; Williams SR
; Martin AV
; Streltsov VA
; Quiney HM
IUCrJ
2016[Mar]; 3
(Pt 2
): 127-38
PMID27006776
show ga
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 powder diffraction data, sharing features of both. The extremely small sizes
of nanocrystals, as well as the possible imperfections of their crystallite
structure, significantly affect the diffraction pattern and raise the question of
how best to extract accurate structure-factor moduli from serial crystallography
data. Here it is demonstrated that whole-pattern fitting techniques established
for one-dimensional powder diffraction analysis can be feasibly extended to
higher dimensions for the analysis of merged SFX diffraction data. It is shown
that for very small crystals, whole-pattern fitting methods are more accurate
than Monte Carlo integration methods that are currently used.