protien crystalography.

WWolfgong wwolfgong at aol.com
Mon Oct 20 14:33:04 EST 1997


I am a staff crystalogapher for a chemistry department. This involves solving
 structures for chemists (molecules which rarely exceed 200 hundred nonhydrogen
 atoms ( this would be the extreme case)). My question is how does protien
 crystallography differ. I understand the resolution is lower (~1.5 angstroms
 versus ~0.8) and that instead of assigning atoms to the difference map, amino
 acid residues asigned instead during refinements of the model. How do you
 chose a residue and what is the justification? For me, I look at bond lengths
 and angles, how could that apply to amino acid residues, I see no relation.
 Also, a good structure for a compound has a R value of less than 6%, I have
 seen publications of protien structures which exceed 30%. What is good for protiens?




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