The source for the X-ray background are points along the air path
post-collimator including the sample with loop and cryoprotecdant (or
capillary and mother liquor). So the 1/r^2 falloff is noticable going from
100 mm to 200 mm. The same counts in a 2x2 pixel area is now seen in a 4x4
pixel
Hi all,
I have a question regarding the methylation of macromolecular complexes. Is
there any report where a macromolecular complex has been successfully
methylated and later on crystallized. Is methylation a method of choice to
chemically modify macromolecular complexes where the entropical
Jim's point is well taken and can perhaps be generalised to say one is
limited either by the crystal or by the set up for recording the
diffraction. To optimise things it is useful to know where the limits
are.
With some tightly focused synchrotron beams you can also see your spots
getting
Jan Rash wrote:
Hi all,
I have a question regarding the methylation of macromolecular
complexes. Is there any report where a macromolecular complex has been
successfully methylated and later on crystallized. Is methylation a
method of choice to chemically modify macromolecular complexes
Hi Jan,
Maybe this link
http://www.jenabioscience.com/cms/en/1/catalog/529_jbs_methylation_kit.html
http://www.jenabioscience.com/cms/en/1/catalog/529_jbs_methylation_kit.html
or these references helps
References
[1] Kim et al. (2008) Large-scale evaluation of protein reductive
Posted on behalf of Lachlan Cranswick:
The Computing Commission and Teaching Commission has produced a joint
November 2009 newsletter on the theme of Age Concern, which deals with
issue concerning the slow march towards retirement of the major
generation of crystallographic programmers, as
Hi all,
I have a small complex, one component is 13 kDa with structure available and
the other is 7 kDa, which could not be able to grew crystals after lots of
efforts. It grew crystals after methylation and diffracted to 2.3 A, however, I
could not be able to solve the structure using
Hi Peter,
How do you know you have crystallized the complex? Perhaps MR is not working
because your crystals only contain the small protein.
good luck,
Eric
Hi all,
I have a small complex, one component is 13 kDa with structure available and
the other is 7 kDa, which could not be able
I have a small complex, one component is 13 kDa with structure available
and the other is 7 kDa, which could not be able to grew crystals after lots
of efforts. It grew crystals after methylation and diffracted to 2.3 A,
however, I could not be able to solve the structure using the structure of
Dear CCP4 community:
I am a beginner to crystallography and therefore my apologies if this question
is too
simple.
Basically we obtained several crystal forms of the same molecule, which is a
hetero-
trimer containing protein A(18kD), protein B(16kD) and a RNA segment(40nt or
about
15kD).
There is a reasonable experiment you can do:
Take the unit cell of your (presumed) crystal complex and put the search model
into the until cell in a way that seems reasonable (use coot, or your favorite
program). Make structure factors (with CCP4 or your favorite program) and throw
away the
Dear CCP4 community:
Sorry if there is a duplicate post. I am a beginner to crystallography and
therefore my
apologies if this question is too simple.
Basically we obtained several crystal forms of the same molecule, which is a
hetero-
trimer containing protein A(18kD), protein B(16kD) and a
Yes,
Ive methylated a ~300 kDa complex once, just for kicks and it still
functioned. MS was fairly good as well, showing that essentially all
accessible amines were altered. Notably I did not get the entire 300 kDa
complex on MS it did not survive TFA/Acetonitrile and I saw components
Hi there,
2 things:
Are you sure that the relative orientations of your components are the same in
the different crystal forms? If you haven't done it already, it would be worth
while trying to search for the individual components as well (could be
difficult because your components are not so
Hi All,
I am using MSD PISA web server to analyze the protein ligand interface in my
newly solved structure. The ligand in the structure is a new inhibitor
(generated using PRODRG), so there is no entry for the inhibitor in the PDB.
Therefore when I am uploading my pdb file to PISA server it is
Hi Koustav,
I had the same question before and here is the answer from Eugene Krissinel,
the developer of PISA:
Yes PISA has a database of compounds, which contains certain interaction
parameters. If a compound is not found in the database, then PISA does not
know how it interacts with other
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