This is a good point - I had thought that D would be very low for an
incomplete shell, but that doesnt seem to be true..
Garib - what do you think?
Eleanor
Petrus H Zwart wrote:
I typically process my data to a maximum I/sig near 1, and
completeness in
the highest resolution shell to 50% or
Qing Xie wrote:
Hi,
I'm trying to get the difference map by subtracting the native
electron density map from the complex electron density map. MAPMASK
has a function of ADD/MULT, but I don't know how to use it?
Any other ways to attack this problem in real space?
Thanks in advance,
Qing
Dear All,
Apologies, this is not MX related, but is important, especially if
you are an industrial user.
From the 1st April 2007, CCLRC will be an ex Research Council. It
is merging with PPARC and becoming Science Technologies Research
Council (STFC). CCLRC will remain a legal entity
Oops (and not object orientated programming either)
Science and Technology Facilities Council (STFC)
Charles
On 23 Mar 2007, at 11:56, Charles Ballard wrote:
Dear All,
Apologies, this is not MX related, but is important, especially if
you are an industrial user.
From the 1st April 2007,
I seem to recall this being discussed at some point.
For the difference electron density map, there clearly isn't a downside to
loss of reflections, i.e., the coefficients in the map generation are
formally zero for Fo-Fc (which all the scaling, weight, sigma-A bits in
there). If the phases are
Dear all,
I have anomalous data from CNS and I have converted them in CCP4 format
with 'cns2mtz' (from Kevin Cowtan). But there are F(+) and F(-) columns,
and I would like use DM which need Fmean only.
Is there an utility in CCP4 which converts F+ and F- to Fmean ?
I have tried mtzMADmod but my
I don't understand why should D be low for an incomplete shell?
According to Randy's tutorial:
D includes effects of:
difference in position or scattering factor
missing atoms
difference in overall scale or B-factor
i.e. all kinds of error in the SF model, but this is surely uncorrelated
with
A great opportunity is on offer to work on one of the most exciting areas of
structural biology - that of integral membrane proteins with a focus on ion
channels and transporters.
Position Title: Postdoctoral Scientist - Membrane Receptor Signalling Group
Grade: Salary scale for
Below is a horrible hack awk script which patches a file of scores into
a PDB file. I'm sure these a nicer way of doing this!
Phil
Is there a program in CCP4 with a command to change
the B-factor of a single residue? I checked the
documentation for pdbset and it seems to assign
B-factors
Hi,
I believe such requirements concern only Nature Methods rather than
Nature by and large.
Regards,
Nadir Mrabet
Pr. Nadir T. Mrabet
Cellular Molecular Biochemistry
INSERM U-724
UHP - Nancy 1, School of Medicine
Avenue de la Foret de Haye, BP 184
54505 Vandoeuvre-les-Nancy
Is there a program in CCP4 with a command to change
the B-factor of a single residue? I checked the
documentation for pdbset and it seems to assign
B-factors only for the whole molecule.
What I'd like to do is plot a given residue property
in a graphic software using the color by b-factor
--- Juergen Bosch [EMAIL PROTECTED] escreveu:
How about Coot ? Click the residue you want to
change and hit Resdiue
Property.
That's how I used to do it, but things start to become
boring when one needs to do it with more than one pdb
file with about 200 residues each. Does coot accept
some
Dear Colleague,
A workshop on coherent x-ray diffractive imaging in biology and
nanoscience will be held at
the 2007 APS Users Meeting. This emerging technique offers an approach
to understanding biological
systems that complements crystallography, EM, and solution x-ray
scattering by its
Dear All,
I got enclusion body in many cases when I tried to express human
proteins in E coli. I would like some suggestions on how to go about
it. I would also like to try co-expression of GroEL/GroES or
DnaJ/DnaK, and would like to know where to get the plasmids.
Any help or comments would be
Hi Weijun,
you can get a kit from Takara (chaperone kit #3340) which has five
different chaperone plasmids (combinations of various chaperone). It
worked for me assofar that I could express huge amounts of the chaperones,
but my target protein was either not expressed at all any more (seems as
if
Weijun,
There are literally hundreds of options you can pursue - obviously a
comprehensive and detailed list of suggestions would not fit in a little
email (in fact they don't all fit into a one-volume book).
It would be helpful to narrow things down a bit - for starters, for one or
two cases
Dear Weijun
Have a look at our REFOLD database - there are some examples of
chaperone assisted refolding as well as many protocols for refolding
of disulphide-rich proteins
http://refold.med.monash.edu.au
good luck
ashley
On 24/03/2007, at 12:23 PM, [EMAIL PROTECTED] wrote:
Hi Weijun,
As has been suggested, you can try
other hosts - for instance Gram positive bacteria (Bacillus megaterium is an
interesting host as are other bacilli, especially if your protein is
secreted), other Gram negative bacteria (Pseudomonas for instance),
Can anyone comment on availability of Archaea
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