On 07/12/2012 10:43, Appu kumar wrote:
Dear Users,
I am refining a enzyme structure with ligand.
I want to make the simulated annealing omit map of ligand including
with 4 Angestron radius around the ligand. I am seeking your valuable
advice to help me out. I know how
I echo with Nat and support depositing both structures. Despite the fact that
the 38 residues are disordered, these are 2 different proteins (chemically).
The disordered residues may not lead to a better model, but they do carry
information. They are there and still take up physical space, thus
Dear all,
I have a data set which is highly anisotropic (3.5-4A in one direction
and 2A in the other) and huge amount of scattering in some rotation
ranges. I know there is the anisotropic correction server which I can
use to do scaling to the weaker data and get it into a kind-of isotropic
I would recommend Modeller
http://www.salilab.org/modeller/
Wai
Suppose I have two proteins A and B, they are structurally homologous,
however the sequence identity is only about 20%. A has crystal
structure available, so if I want to model protein B, what's the best
way to do it? I don't thin
Dear All,
Does anybody has any comment on using heparin as an additive to
co-crystallise an RNA-binding protein? I am not asking about using it
to form a complex with proteins that are know to bind heparin
specifically, but using it as a general RNA analogue, when we lack the
knowledge of th
