-----BEGIN PGP SIGNED MESSAGE----- Hash: SHA1 Dear,
1.24A resolution is reasonable for anisotropic refinement - including restraints you have more observations than the number of reflections, so just doing the calculation does not give a concise answer! You should try and see if the refinement is stable and makes sense (e.g. check the number of npd-atoms etc.) You may also try the RIGU command in the beta-version of shelxl (Acta Cryst. (2012). A68, 448-451)! Regards, Tim On 09/17/2012 08:31 PM, Yuri Pompeu wrote: > Dear community, > > The protein model I am refining has 400 amino acids (3320 atoms). > Some real quick calculations tell me that to properly refine it > anisotropically, I would need 119,520 observations. Given my > unit-cell dimension and space-group it is equivalent to about a > 1.24 A complete data set. However, I have had a couple of cases > where anisotropic B-factor refinement significantly improved > R-work and R-free, while maintaining a reasonable gap for lower > resolution models (1.4-1.5 A, around 70,000 reflections). What is > the proper way of modelling the B-factors? Any thoughts and/or > opinions from the community are welcome. Cheers, > - -- Dr Tim Gruene Institut fuer anorganische Chemie Tammannstr. 4 D-37077 Goettingen GPG Key ID = A46BEE1A -----BEGIN PGP SIGNATURE----- Version: GnuPG v1.4.12 (GNU/Linux) Comment: Using GnuPG with Mozilla - http://enigmail.mozdev.org/ iD8DBQFQV284UxlJ7aRr7hoRAh5FAJ43TevZbbQLYGeE1yM2cqKjZ5KMFACg5bCs Ijn4owVvuuHldNSnK4Iax1E= =4Jdg -----END PGP SIGNATURE-----
