Gentle reminder of the following openings at SGC Oxford (deadline 7th
February noon). Thanks.
On 14 January 2013 17:51, Wyatt W. Yue yuewai...@googlemail.com wrote:
Dear all,
We are seeking two post-doc scientists in the Metabolic Rare Diseases
group at the Structural Genomics Consortium
Just to add some more possibilities:
- You can download maps from EDS or models and maps from PDB_REDO straight into
CCP4mg.
- You can download PDB_REDO maps and models into PyMOL using this plugin
(http://www.cmbi.ru.nl/pdb_redo/pymol.html) for which we should thank Ed
Pozharski. Note that
Dear all,
sorry for the semi-off-topic but I'm trying to help convert some diffraction
images and this seemed like a good place to ask. We are trying to process some
images collected on a Pilatus 300K with the Crysalis Pro software (small
molecule) but it seems to only be able to read Pilatus
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Dear Jose,
it is odd the software should read 6M but not 0.3M Pilatus files - the
format is probably the same, only the dimensions would differ - at
least that's my guess.
While you are waiting you might start processing your data with XDS,
which is
Hi Tim
I've looked at these images and they differ from the normal 6M images
(miniCBF) in that they are a stab at writing fullCBF, i.e. with
imgCIF style data content - unfortunately, there are a few syntax
errors which need fixing before programs that use the header
information (like
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Hello Xavier,
if you look at the downloaded file, you'll notice the source of the
error: The pdbe download link has changed, i.e. this is not a
PDB-file. You'll have to download the PDB file manually until it is
fixed in the latest coot-code.
Dear All,
I am trying to probe the existence of a disulfide bond on the surface of my
protein.
I have attempted Ellman´s and my results were not as clear as I would have
hoped for.
I am not a sulfur/cysteine chemist and would appreciate the advice on what
experiments to try!
Thanks a bunch
YAP
I never done such experiments but N-Ethylmaleimide labeling and Mass-Spec could
be the solution.
Le 6 févr. 2013 à 17:10, Yuri Pompeu yuri.pom...@ufl.edu a écrit :
Dear All,
I am trying to probe the existence of a disulfide bond on the surface of my
protein.
I have attempted Ellman´s and
===
SYNCHROTRON BEAM TIME FOR MACROMOLECULAR CRYSTALLOGRAPHY AT SLS
===
Proposal application deadline: Friday, February 15, 2013
Periods:
May 1, 2013 - August
Hi,
to my knowledge, Ellman's reagent detects free thiols only. (Or am I
wrong?) In contrast, with the method of Thannhauser (Thannhauser [1987],
Methods Enzymol. 143, 115-9) you can determine the total amount of thiols
(free and in disulfide bonds). Any difference between the two methods
Couldn't you just run reducing/non-reducing SDS-PAGE lanes and see the
difference?
JPK
On Wed, Feb 6, 2013 at 11:10 AM, Yuri Pompeu yuri.pom...@ufl.edu wrote:
Dear All,
I am trying to probe the existence of a disulfide bond on the surface of
my protein.
I have attempted Ellman´s and my
Does that CA have a metal center (I think they all do)? If so, doesn't the
citrate compete for the metal?
JPK
On Mon, Feb 4, 2013 at 2:25 PM, Roger Rowlett rrowl...@colgate.edu wrote:
Human carbonic anhdyrase II can be easily crystallized from 1.3 M sodium
citrate/0.1 M TrisCl pH 8.5 at 10
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Dear Yuri,
If you have access to mass spec, this should be a straight forward experiment.
Find the
reference here.
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