I don't know what this error is, but you might like to know that the
program Pointless can be used as
an alternative to sortmtz, with the bonus that it might help you
determine the spacegroup
You can get it either from our ftp site here
eg
OK, that's a good question. Unfortunately the answer is hard, otherwise
I would have done it already.
The a[] and b[] coeffs are the Gaussian coefficients used for
calculating an atomic shape function in reciprocal space, i.e. for use
in a structure factor calculation.
The aw[] and bw[]
Dear all,
When running Pointless 1.2.0 (see summary below), I get the cubic
space group P 4 3 2
(mosflm gave P 2 3 or P 4 3 2)
!--SUMMARY_BEGIN--
Best Solution space group P 4 3 2
Reindex operator: [h,k,l]
Laue group probability: 1.000
Systematic absence
Dear all,
When running Pointless 1.2.0 (see summary below), I get the cubic
space group P 4 3 2
(mosflm gave P 2 3 or P 4 3 2)
!--SUMMARY_BEGIN--
Best Solution space group P 4 3 2
Reindex operator: [h,k,l]
Laue group probability: 1.000
Systematic absence
Dear Kristof,
I recently had lots of trouble with molrep in space group
F432. Both Phaser and Molrep failed, only Amore produced
a solution.
Hope that helps.
Manfred.
*
You should certainly try the other P 4x 3 2 space groups (x=1,2,3) in
case the assignment of screw axes is wrong
Phil
On 13 Nov 2007, at 13:17, Kristof Van Hecke wrote:
Dear all,
When running Pointless 1.2.0 (see summary below), I get the cubic
space group P 4 3 2
(mosflm gave P 2 3
Dont forget pointless gives a point group so you could have spacegroup
P4123 too - check that in MR
Could might well have a trimer sitting on the cubic 3-fold, but then the
oligimer will be generated by the crystal symmetry, and you need only
search with a monomer.
Eleanor
Kristof Van
On Tuesday 13 November 2007 06:41, Brad Bennett wrote:
I would be interested then to know how the community feels about the
correlation of B-factors to protein flexibility. It is generally accepted
that these are linked but are there any new papers that address this?
This is the basis of
Dear Brad,
the flexibility, that is how far a protein is stabilized with cold and heat
denaturation of a protein,
this inturn depends on
1.solvation enthalpy of nonpolar moieties(need more energy,so there needs to
be some randomness)
2.shift in temparature due to the enthalpy associated with
*A post-doc position and a PhD position in structural biology is
available in the group of *
*Prof. Dietmar A. Plattner*
*at*
*Institute of Organic Chemistry and Biochemistry,
Albert-Ludwigs-University Freiburg/Germany*
The project involves investigations of structure-function relationships
Somebody out there who could direct me to
a nice review of protein powder diffractometry
including the application of Rietveld refinement
to such data.
Any hint appreciated
many thanks in advance
Marius
Dr.habil. Marius Schmidt
Asst. Professor
University of Wisconsin-Milwaukee
Department of
Hi
I don't know about reviews, but there were a couple of papers a few
years ago that might have clues in their references -
Margiolaki et al, Acta Cryst D61, 423-432 (2005)
Basso et al Acta Cryst D61, 1612-1625 (2005)
On 13 Nov 2007, at 19:59, Marius Schmidt wrote:
Somebody out there who
Diffraction from protein powder is a relatively new
development which requires the beam properties of
synchrotrons. As you know, of course, the number
of Debye-Scherrer rings are increasing dramatically
with diffraction angle. Since proteins have such
a large unit cell, the reflections are very
This may not apply in your case but it is not uncommon for a protein to
precipitate in a microcrystalline shower when put in cold. Once it
worms up, the crystals dissolve and the precipitate clears up. It is
easy to check under a high magnification microscope.
Cheers,
N.
Ruslan Sanishvili
Did you check the pH of your DTT and the protein solution before and after?
I have had some experience with DTT changing pH (as might well be
expected...).
Jacob
***
Jacob Pearson Keller
Northwestern University
Medical Scientist Training Program
Dallos
The other possibility is 400 mM imidazole in the buffer. The
precipitate looks like silk.
On 11/13/07, Bryan W. Lepore [EMAIL PROTECTED] wrote:
you didn't say how you know its protein - is it?
interesting though.
It did not contain DTT when frozen.
On 11/13/07, deena [EMAIL PROTECTED] wrote:
Are you sure its 1mM DTT, because DTT itself precipitates in the freezer.
Deena
On Nov 13, 2007, at 3:30 PM, Joe wrote:
Hi there,
I see enormous precipitate of my receptor protein when I take it out
of
The precipitate does not disappear automaticly if I don't add DTT.
If it's the precipitate of imidazole, then why DTT can dissolve it?
thanks
On 11/13/07, Sanishvili, Ruslan [EMAIL PROTECTED] wrote:
This may not apply in your case but it is not uncommon for a protein to
precipitate in a
i can't seem to find any reviews that specifically consider how NCS
influences space group / symmetry determination - though there are plenty
individual accounts.
can anyone cite a review or even a book chapter on such a topic? or maybe
even some cases of non-obvious indexing errors? of
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