If a pdb file contains some residues that have multiple conformations,
when using refmac to refine it, will the programm take consider of
these conformations? It seems that refmac would do this but I am not
very sure. I downloaded a structure with some conformations from the
pdb, but after refm
Dear John,
I think it may necessary to collect all satellites corresponding to the 256
Angstrom axis in order to solve the structure correctly. In small-molecular
crystallography there is already straightforward way of solving
superstructures: Derive phases of main reflections (corresponding to
Hi
For your SAD / MAD data, firstly after merging can you see any peaks in the
anomolous difference patterson map - this is critical. You could try using
SOLVE / RESOLVE or SHARP / AUTOSHARP to identify sites and to calculate phases,
as you have a little bit more control over the process. You
So far, the native crystals diffracted best to 2.4A. The MAD data
diffracted to 2.6~2.7A. We attempted to use phenix.hyss to identify copper
atoms, and the program had hard time to identify the sites.
The protein: Cu ratio is around 1:1, which is decided by ICP-AES measurement
of the crystalliza
It would be useful to know how you tried to solve the structure by MR.
Just because there is a large number of chains in the ASU isn't a reason
that MR will fail. At times you need to find some of the chains, do some
rebuilding, and then use that amended model for a continued search.
Bernie Santar
Hi:
Is the resolution of the data sufficient to apply direct methods to find
only the copper atoms, then use the copper atom positions in an
old-fashioned
'heavy-atom' phasing method, combined with direct methods?
Incidentally, was the following publication of any relevance in your
effort
Dear all:
We already got nice crystals of a drug-protein complex, however, MR
failed due to the huge copies (>12) of protein molecules per asu. Protein
itself is a small one, only ~70 aa.
Later on, we collected MAD data of copper (copper : protein ~ 1: 1),
Rsym of the data was around ~9%
Dear Colleagues,
I am currently engaged analysing a protein crystal structure which has two
unusual aspects about it, at least to me (hence this consultation).
The first oddity is the unit cell and space group:-
Triclinic P1 64.43 70.81 79.26 89.83 110.95 116.59
ie note the value of alp
Applicants interested in one of the positions listed below are invited
to send their complete resumé (indicating the position of interest and
including the names of three possible referees), before April 16, 2007, to:
Universität zu Lübeck
Dezernat Personal
Ratzeburger Allee 160
23538 Lübeck
Furt
Please would you bring this to the attention of any suitable candidates looking
for a postdoc position. Thanks, John
An opportunity exists to join a team studying proteins involved in homologous
DNA recombination in the group of Dr John Rafferty in the Krebs Institute, Dept
Mol.Biol. & Biotech. a
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