In article <3glegb$56a at lyra.csx.cam.ac.uk>, owde100 at bioc.cam.ac.uk (Orhan Ertughrul) writes:
|> In article <1995Jan30.201542.18484 at alw.nih.gov>, johnk at spasm.niddk.nih.gov (John Kuszewski) writes:
|> > In article <3ggmdi$5j at mace.cc.purdue.edu>, barani at mace.cc.purdue.edu (Barani) writes:
|> > |> IMHO crystallographers are more closer to the truths
|> > |> of a biomolecule than anyone else.
|> >
|> > Except, of course, for us NMR people. No packing distotions,
|> > good pictures of flexibility.
|> And a residue limit of about 250AA even for 4D. NMR is always going to be a
|> technique of restricted use until larger biomolecules can be resolved.
But then again, any technique is of restricted use (ever tried to crystallize
and solve a G-protein coupled receptor, I guess we'll leave that to the EM
people). Let us not argue about which technique is best, each of them,
including modelling, can give us a new perspective on the complex problems
we are facing: why are proteins folded they way they are and why do they function as they do.. I got my PhD in bio-NMR and modelling and am currently working in a bio-X-ray lab. I feel all three techniques are interesting and useful but not perfect. Let's try to learn from each other instead of putting
each other down.
Just my $0.02,
Ronald
