Hi,
The situation is somewhat like my case. Have you checked the purity level of
the protein in SDS PAGE. In that case you may try to introduce another
purification step.
regards
Debajyoti
On Fri, 05 Feb 2010 10:05:23 +0530 wrote
>Hi, All,
We are trying to crystallize a protein
> My interpretation of hollow crystals is that the crystals are growing too
fast.
This is indeed true and a well known effect observed also in mineral
crystals,
namely that the edges grow fastest and the faces fail to fill (or the
crystals
are filled with disordered material. The examples are the
My interpretation of hollow crystals is that the crystals are growing
too fast. I've had success with similar looking crystals by slowing
crystal growth. You can try lower temperature, protein concentration,
or precipitant. In my case, I found success by trying different
concentrations of NaCl in t
I have just noticed that there is a definitive table of equivalent
origins for all 230 space groups in volume B of International
Tables (in Chapter 2.2 by Carmelo Giacovazzo). This appears to
agree with Ian's last email in this thread for the space groups
discussed there. It gives the origins dire
On Thu, Feb 4, 2010 at 2:52 PM, Mark A. White wrote:
> Hello,
>
> Does anyone know why COOT is suddenly as slow as molasses on my Fedora 12
> desktop? I had and old version of Coot working after my initial Fedora 12
> install (from FC7 after a disk crash). However, now all versions of COOT
> h
Dear All,
Attached is information about a new X-ray crystallography training program
being introduced at Pennsylvania State University. Kindly pass it along to
anybody that may be interested in such an oppurtunity. Thank you
Neela
<>
A postdoctoral position is available to study the structure of diverse
drug targets in the laboratory of Dr. Barry Finzel in Department of
Medicinal Chemistry at the University of Minnesota Twin Cities Campus.
Current research in the Finzel laboratory includes a diverse portfolio
of targets
Hello,
I have a SeMet-SAD dataset (at Br edge : 2.7 A) and a 2 wavelength MAD
dataset (inflexion and remote : 3 A). The SAD dataset when searched for
heavy atom sites with a native dataset (SIRAS) gives a figure of merit of
0.26 and Z-score of 28. The MAD dataset by itself gives a low figure of
me
Hello,
I have a SeMet-SAD dataset (at Br edge : 2.7 A) and a 2 wavelength MAD
dataset (inflexion and remote : 3 A). The SAD dataset when searched for
heavy atom sites with a native dataset (SIRAS) gives a figure of merit of
0.26 and Z-score of 28. The MAD dataset by itself gives a low figure of
me
Hello,
I have a SeMet-SAD dataset (at Br edge : 2.7 A) and a 2 wavelength MAD
dataset (inflexion and remote : 3 A). The SAD dataset when searched for
heavy atom sites with a native dataset (SIRAS) gives a figure of merit of
0.26 and Z-score of 28. The MAD dataset by itself gives a low figure of
me
Rui--
It is not uncommon to see "hollowed ends" on crystals when they grow
quickly at that point. You have received some very good suggestions thus
far, and slowing down the growth might also be helpful. We have had good
success doing this by just varying the protein concentration and/or the
Three Year Postdoctoral Position in Protein-DNA Crystallography,
Institute of Biomedical and Biomolecular Sciences,
University of Portsmouth, U.K.
Salary from £31,671 per annum.
The Biophysics Laboratories are very well equipped for structural and
molecular biology and house a number of groups wi
Here is Randy's reply:
Dear Hari,
Well, it turns out to be a combination of some bad data and a
poorly-considered feature in Phaser.
Something must have gone wrong with the data from 2.9 to 2.8A, because
the intensities are much too large. I've been developing a new
relative Wilson plot tool to
Dear Rui,
Perhaps this is another instance where the PX Scanner might prove
so helpful ? Maybe, amongst your many crystals - all of which 'look'
not too bad ... there are one or two which actually diffract much further
beyond the 2.9Å which you mentioned ? However, unfortuna
As a complement to the earlier comments from George:
CrysAlisPro is the name Oxford Diffraction uses to describe their
instrument control and
data reduction software; it writes out frames in Oxford format and can
convert its frames
to XDS, (i)MOSFLM and MAR compatible formats. In
On Fri, Feb 05, 2010 at 12:23:13PM +, Frank von Delft wrote:
> Or should I say: it works better for *me*. All other scaling programs
> are more terse than scala, but maybe I've just never figured out where
> to look.
I think you should say *me*. I like the postscript plots sadabs produces
On Fri, 05 Feb 2010 05:39:14 +0100, rui wrote:
Hi, All,
We are trying to crystallize a protein and found some initial hit in the
following conditions,
pH 4.8, 0.2 M AS or some other salts ( NaCl,LiCl, MgCl2 ), 32% PEG4000 or
PEG3350 ). However the quality of the crystal is not so great,some o
One thing that is superior is that the scala output gives you a better
feel for the data quality, especially thanks to the per-image plots, for
things like B-factor decay.
Or should I say: it works better for *me*. All other scaling programs
are more terse than scala, but maybe I've just nev
In all versions of Phaser up to the currently distributed ones, the assumed RMS
error of the model is used to generate an a priori SigmaA curve for the
likelihood target. At the end of the structure solution, the map coefficients
are computed by using those a priori SigmaA values to calculate m
On 5 Feb 2010, at 10:35, George M. Sheldrick wrote:
> PROTEUM (and APEX) are the names Bruker uses to describe the instrument
> control software; they write out frames in Bruker format. In the standard
> Bruker system the frames are integrated by SAINT which outputs reflection
> records in Bruker
PROTEUM (and APEX) are the names Bruker uses to describe the instrument
control software; they write out frames in Bruker format. In the standard
Bruker system the frames are integrated by SAINT which outputs reflection
records in Bruker .raw format (not to be confused with a different .raw
forma
The latest latest version of Pointless from our ftp server here will convert
output from SAINT to mtz for input into Scala etc. I'm guessing that Proteum X8
is the same as SAINT (is it?)
Phil
I've done some work on Pointless & Scala to try to make them work properly for
Saint Phi scans,
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