Hi
Intrinsic fluorescence may be used to monitor such change qualitatively.
Another option is red-edge excitation flourescence technique may work if
there are suitable fluorophores (W or F) on the each of the two domains
changing solvent accessibility upon rigid body motion.
Amit.
On Mon, Dec
Dear all, we have a vacancy for a postdoc within the MX group at Diamond. Full
details can be found at
http://www.diamond.ac.uk/Home/Jobs/Current/DIA0584-TH.html. Interested
candidates can contact me directly by email for further details on research
project associated with the post
Martin
I would like to point out that HSQC could still be applied even in such a large
protein. TROSY-HSQC has been successful in improving peaks in spectra of large
protein. Typically the sample would need to be deuterated to see the full
effect of TROSY, but even a partial deuteration can improve
I agree - looks like small molecular diffraction.
Try increasing delta-phi to catch more of the lattice to confirm - I
often do a 5º image or two with the detector pushed as close as
possible to check for salt diffraction when screening.
The lack of low res (~15-20Å) spots around the beamstop is
Dear colleagues,
Since January 2010, the BM14 MAD MX beamline at the ESRF (Grenoble, France)
is providing beamtime for both European and Indian MX communities after a
smooth transition from the UK MRC-EMBL tandem to the actual
EMBL-ESRF-India consortium.
The beamline is fully opened now
Definitely small molecule crystals. You might want to push the
detector closer and use better cryo solution for further confirmation.
Nian
On Tue, Dec 7, 2010 at 8:14 AM, xiuwen zhang congru...@gmail.com wrote:
Dear Colleagues,
Currently we got several very tiny crystals. After exposuring
Hi there:
The situation: We are facing difficult molecular replacement: we believe
we have two molecules in the ASU, but phaser/molrep find only one. Using
the electron density calculated using this single molecule, we have
manually placed the 2nd molecule, albeit not good enough for rigid
Just a thought:
shave off parts of your model1, which you think might cause a clash perhaps,
essentially keeping a core in place, then rerun molrep using model1 as fixed
and search for a second. If you are successful, then SSM superimpose your
complete model onto both and see what you have to
Try this, assuming you have good data. Use one molecule you got to do
refinement (rigid body or restraint refinement with tight restraint)
and phase the map. Then do a phased map molecular replacement. You
might want only use the core of your protein to do the molecular
replacement search to
Dear all,
Recently I collected several data sets at 13B1 Taiwan beamline with Q315r
detector. It's no problem to index these datasets using mosflm, but Rms
residual and weighted residual is high. Here I want to try XDS to play my
data. I downloaded a template example as below.
Look into the header of your image file via more or run mosflm on one image and
look at the output in the terminal window.
You'll get the pixelsize and you'll need to convert the beamcenter into pixels
from mosflm. Keep in mind that beam X = orgy in xds and beam y is orgx
Plus the usual stuff
Donghui,
there are several ways to get ORGX ORGY parameters. As Juergen suggested,
you could use the numbers from the header or Mosflm output.
More information on the excellent XDS Wiki:
http://strucbio.biologie.uni-konstanz.de/xdswiki/index.php/Obtaining_ORGX_ORGY
Another option would be to
Dear all,
I would like to make a picture of diffraction photograph with (hkl) indexes.
I found it in Fig. 1 in the paper: Acta Cryst. (2009). D65, 553-559
http://dx.doi.org/10.1107/S0907444909010725
Direct link to the figure:
http://journals.iucr.org/d/issues/2009/06/00/dz5158/dz5158fig1.html
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