If you are seeing waters at 4 A you are probably looking at ions.
Those are OK to model, but definitely try occupancy refinement from a
variety of starting points to make sure you are not fooling yourself.
Occupancy refinement might also help you assign which ion it is. That,
and some
The REFMAC option of NCS Local restraints checks how closely your subunits
match and adjust the spans of residues restrained accordingly. So if a
helix has moved relative to the main body of the molecule, restraints will
still be applied but with an adjusting fit.
That works very well in general.
Postdoctoral Research Assistant in Molecular Modelling and Simulation of
Compensatory Mechanisms in Proteins at Queen Mary University of London
(deadline 30 April 2015)
We wish to recruit a Postdoctoral Research Assistant to work in the research
group of Dr. Arianna Fornili in the School of
Dear CCP4BB,
The DIALS team will be running a workshop at ECM29 this summer - more
information can be found at:
http://www.diamond.ac.uk/Home/Events/2015/Satellite-meetings-at-the-ECM.html
and is copied below. Registration is through the usual ECM registration
process. We look forward to seeing
Hi,
I agree with Kay, try to fry your native crystals to get the highest overall
resolution possible, but go for low resolution if your crystals decay rapidly,
particularly when collecting anomalous data. A high overall resolution is
always desirable, but during anomalous phasing you can
Just to clarify, I think what Kay meant with strategy is that you don't just
shoot at the crystal and collect. You should figure out what is the optimum
start and end point of your data collection. Best to be cautious and not
immediately go for highest resolution and not fry your crystal. A 4 A
Something else you could try is using a kappa goniometer. There were a couple
of presentations at the last CCP4 meeting where they discussed that alignment
along the appropriate axis using a Kappa goniometer often worked much better
than the inverse beam mode. By aligning the crystal with the
I would disagree.
My philosophy is: assume this is your only diffracting crystal, maximize the
outcome by investing some thoughts into it before being sorry. Therefore, run
strategy and optimize for anomalous pairs being collected as close in time as
possible.
If you have the luxury of having
Hi,
I'd say using a Pilatus detector in fine-slicing mode and lowdose/high
multiplicity will give you better chances to solve the structure. The right
strategy makes a difference ...
Best,
Kay
But if you only have a single diffracting crystal, then you don't know the
space group before the experiment, and you have to collect 180 (native) or 360
(anom) anyway.
Plus, I have seen too many sorry cases where people thought they had a certain
space group, and later it turned out to be
Finally, there is simply no downside in collecting more degrees with
proportionally lower dose on the Pilatus. Merging the data recovers the _same_
signal. It has only advantages - so many that I won't write them up here with
1 finger on my tablet.
...Up to the point at which one can no longer
I’m sure James Holton has an option for that :-)
By the way, zero photon data sets exist and have been published before (some of
them had to be retracted though).
Jürgen
..
Jürgen Bosch
Johns Hopkins University
Bloomberg School of Public Health
Department of Biochemistry
Sorry for an off-topic question. We are seeking a new DLS(Dynamic Light
Scattering) instrument which is best for our needs. Any suggestion to a
traditional structural biology lab? The make, model #? Any suggestion will
be very appreciated. Thank you!
Best,
Adam
Hi,
Re Has anybody ever used xenon? Can anyone share the starting pressure
and time for optimization?
This paper :-
doi:10.1107/S0907444901009350 http://dx.doi.org/10.1107/S0907444901009350
offers you details.
Best wishes,
John
On Fri, Apr 17, 2015 at 2:11 AM, joy yang joybeiy...@gmail.com
John, the lower-resolution datasets in your paper were generated by truncating
a high-res dataset, i.e. the lo-res datasets are of great quality. Would the
conclusions still be valid if the data are true low-res? (i.e. I/sigI 1.5-2
in last shell)?
Tx Bert
From:
Hi,
This paper:-
doi:10.1107/S0907444903004219 http://dx.doi.org/10.1107/S0907444903004219
I think will be of interest.
Whilst 4 Angstrom resolution is not covered the article will indicate the
tests you could make to evaluate your 'possible water like densities'.
Best wishes,
John
On Mon, Apr
Dear Colleagues
As part of Bruker's continuing webinar series focusing on techniques in
structural biology, Dr. Robert Rambo from the Diamond Light Source will
present a 45 minute interactive
webinar entitled Assessing Sample Quality for Modeling BioSAXS Experiments
Using ScÅtter. Solution
Hello,
John, the lower-resolution datasets in your paper were generated by
truncating a high-res dataset, i.e. the lo-res datasets are of great
quality. Would the conclusions still be valid if the data are true
low-res? (i.e. I/sigI 1.5-2 in last shell)?
genuinely low-res data set is
Wyatt DynaPro and analogs work well for us. However you're not very
specific what your needs might be :)
Artem
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On Fri, Apr 17, 2015 at 1:36 PM, Tianyu Wang adams.wan...@gmail.com wrote:
Sorry for an off-topic question. We are seeking a new DLS(Dynamic
Dear all,
I thank you all for your kind suggestions and remarks. So the bottom line
appeared to me is - one should not pick water molecules at low resolution
(grater than 3.0/3.5A) data (not a truncated data I guess) unless there is
sufficient reasons/evidences (like presence of water molecules
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