[Protein-crystallography] resolution range for refinement
iulek at uepg.br
Fri Jun 30 13:19:53 EST 2006
You should prefer to use the 20-2.37 A range unless you made some
mistake at measuring your low resolution data or for any reason they were
not scaled properly. But, at doing using this range, you must include a bulk
solvent model into your structure. Did you do so ?
BTW, it seems that the ccp4bb is much more active on discussing protein
crystallography. I wonder how much this xtal-log forum is active !
----- Original Message -----
From: "hothot c" <crzeus at hotmail.com>
To: <xtal-log at magpie.bio.indiana.edu>
Sent: Thursday, June 29, 2006 4:40 PM
Subject: [Protein-crystallography] resolution range for refinement
> Dear all:
> I'm refining a protein structure complexed with an inhibitor. I found
> that if I refine the structure in the range from 20 to 2.37 angstrom, I
> can see a strong positive density in fo-fc map in the second binding
> site,However,if I choose to refine it in 10-2.37 range, this peak is
> nearly invisible.
> What's going on here?Which one should I trust, the more complete one?
> Xtal-log mailing list
> Xtal-log at net.bio.net
More information about the Xtal-log