I am fairly new to protein crystallography so I hope this is not a
silly question. It relates to Bragg's Law. If it is expressed in the
form
n(\lamba) = 2d sin(\theta)
where (\lamba) is the wavelength, d is the separation of the crystal
layers and (\theta) is the angle of incidence and angle of reflection.
This could be rewritten as
(\theta)=arcsine((n(\lamba))/(2d))
This suggests that a diffraction pattern is formed.
My question is this. What would be the practical advantages of
increasing the number of n values that are used to reconstruct the
structre of the protein? IOW, would there be an advantage to
retrieving returns from more (\theta) angles whose sine values are
integral multiples of one another? Can someone suggest some
literature about this?
Many thanks in advance,
Peter.
