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/
____________________________________________




More information about the Xtal-log mailing list