Protein Refinement Methods
islam
islam at icrf.icnet.uk
Thu Mar 4 06:37:52 EST 1999
I have a question (regarding systematic/random errors in
crystallographic structures) which has been bothering me for a while:
Suppose a raw dataset (i.e. just the collected x-ray data) was given
to a number of different Labs to solve. What variation would you expect
in the final results (i.e. x,y,z,bval,rfactor,occ etc) ? Different
groups may or may not be using the same refinement programs. Also
variation in results may also be dependent upon the resolution of the
x-ray data.
(I know that there are a number of cases where the same protein has been
crystallized in different crystal forms, but my question is not
addressing this.)
I hope this is not a silly question to ask ! If it has already been
addressed, I would
be grateful for the references.
Thanks
____________________________________________
Suhail A Islam
Biomolecular Modelling Laboratory
Imperial Cancer Research Fund, P.O. Box 123
44 Lincoln's Inn Fields, London WC2A 3PX
Tel: (0171) 269 3380
Fax: (0171) 269 3258
email: islam at icrf.icnet.uk
http://www.icnet.uk/bmm/
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