Dear CCP4BB members,
We invite applications for two PhD positions in structural cell biology
based partly or entirely at the Astbury Centre for Structural Molecular
Biology, University of Leeds:
- *The structure and function of retinal photoreceptor connecting cilium
proteins (**Closing date:
Hello everyone,
Please see the job advert below regarding tenure-track academic fellowships
in structural molecular biology at the University of Leeds.
Cheers,
Joe
Dear All,
A number of tenure-track academic fellowships in Structural Molecular
Biology are now available at the University of
Dear All,
A post-doctoral position is available immediately in the laboratory of Dr
Joe Cockburn, at the Astbury Centre, University of Leeds, UK to perform
structure-function studies on ciliary transition zone proteins. The
transition zone consists of several large multi-protein complexes at the
Dear All,
A post-doctoral position is available immediately in the laboratory of Dr
Joe Cockburn, at the Astbury Centre, University of Leeds, UK to perform
structure-function studies on ciliary proteins.
The position is funded by The Wellcome Trust and is available immediately
for a period of
Dear BB,
We are trying to solve the structure of a complex between two proteins. We
have two crystal forms of the complex, and a partial MR solution in each.
We now want to average the density between these two forms to improve the
maps, using DMMULTI. However, there are a couple of things I don't
I agree with Randy Read though - it's a mistake to get too carried away
with the foul-play aspect of this. There were clearly very serious
problems with those structures anyway. What it shows is that you can
desposit just about anything in the PDB, which is quite worrying when you
consider how much
Hi Andrew,
If there is no *protein* model built into this region of the map, then it
will be modelled by the bulk solvent correction - therefore, the negative
peaks are telling you that the mean electron density there is lower than
in the bulk solvent. Probably.
Joe
> Hello everyone I have a ques
Dear Richard,
I *think* it works like this, don't know if it's detailed or rigourous
enough for you!
If I(l,h,i) is the intensity of the ith observation of reflection h on
frame l, with error sig(l,h,i), and S(l) is the (inverse) scale factor to
be applied to frame l, then the error in the scaled
Dear Richard,
I *think* it works like this, don't know if it's detailed or rigourous
enough for you!
If I(l,h,i) is the intensity of the ith observation of reflection h on
frame l, with error sig(l,h,i), and S(l) is the (inverse) scale factor to
be applied to frame l, then the error in the scaled
Hi Matt,
I sometimes see a similar thing with my proteins, which definitely don't
possess metal co-factors or prosthetic groups. I found that gel filtration
got rid of it - the browny-yellow stuff came out in the void fraction so I
figured it was aggregated protein. I think it was aggregation via t
Dear Mona,
Yes. You can get Denzo to reject reflections on or close to ice rings, or
any other features with highly irregular background variations, by
increasing the value of the REJECT keyword (see p. 40 of the HKL2000
manual by D. Gerwith,
http://www.hkl-xray.com/hkl_web1/hkl/manual_online.pdf).
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