Dear cryo-EM community,
Two continuing, full time positions are available at the University of
Wollongong in Australia:
Staff Scientist (Cryo-Electron Microscopy):
http://uow.employment.com.au/jobs/Staff-Scientist--Cryo-Electron-Microscopy-/2487
Senior Lecturer / Associate Professor (Cryo-
On Monday, 21 November 2016 11:53:22 PM Seok-Yong Lee wrote:
> Hi All,
>
> We have recently solved several structures of a membrane protein in slightly
> different conformations at low resolutions (3.9-4.2 A). We would like to see
> that these structures reflect truly different conformations and
Hi All,
We have recently solved several structures of a membrane protein in slightly
different conformations at low resolutions (3.9-4.2 A). We would like to see
that these structures reflect truly different conformations and to what extent
these structures are discernible. To answer this quest
Hi,
Well, sometimes proteins don't express even though they are from the same
family and their "cousin" behaved very well.
I found the followings helpful:
1. forget about the concept "this special strain *should* work because it is a
Rosseta/ pLysS etc." Sometimes it's a long mRNA, sometimes a r
We have been expressing a family of human proteins as inclusion bodies in E.
coli, which we can be refolded and crystallized. However, three members show no
expression either as inclusion bodies or as soluble proteins.
The genes were ligated into the pE21d vector with either a His-tag or no
Hi
Hi,
I do this by editor (and cut / paste). Clumsy but works. Let me know if you find a more elegant way.
Cheers,
Boaz
Original message
From: Wei Wang
Date: 21/11/2016 19:05 (GMT+02:00)
To: CCP4BB@JISCMAIL.AC.UK
Subject: Re: [ccp4bb] XDS questions
My personal test
My personal test shows that the different paths vary little with each
other, as long as the scaling is done only once. Another way could be what
is said on XDSwiki: Minimum I/Sigma=50, CORRECTIONS=MODULATION, NBATCH=1.
Then the XDS_ASCII.HKL is handed over to Aimless with default settings.
One que
** X-ray crystallography and biophysics facility manager **
The Max Planck Institute of Molecular Physiology, Dortmund, Germany, is
looking for a X-ray crystallography and biophysics facility manager.
The ideal candidate for this position should have a PhD degree in
macromolecular crystallogr
XDS-CORRECT and Aimless use
1. different scaling models - CORRECT includes a poorly documented correction
across the detector plane not present in Aimless: this may or may not be a Good
Thing
2. different outlier rejection algorithms - XDS seems to reject more
observations
3. different “corr
Dear All,
I agree with Tim - what I was getting at was to perform the scaling exactly
once - i.e. with AIMLESS or XDS CORRECT but not both
The behaviour Tim describes below is exactly what xia2 does :)
Best wishes Graeme
-Original Message-
From: CCP4 bulletin board [mailto:CCP4BB@JISCM
Dear Nishant,
XDS_ASCII.HKL contains corrected, scaled, but not merged reflections.
You can specifically ask XDS to merge your data, but I would not do so unless
really necessary - you loose a lot of information.
I would like to offer a different opinion to Graeme's:
You can read XDS_ASCII.HKL
Dear Nishant
Your statistics will be better taking XDS_ASCII because the scaling has been
performed twice i.e. you have had two goes (with different models) of reducing
the differences between reflections. This will *always* make the R factors etc
smaller – whether the data are better or more t
Dear All,
Just to understand more, the XDS_ASCII.HKL file generated after running XDS
contains scaled and merged reflections?
Moreover, what happens exactly, if you use XDS_ASCII.HKL file in AIMLESS
instead of INTEGRATE.HKL file??
I ran AIMLESS separately, one using already scaled XDS_ASCII.HKL
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