Dear Huiying,
my first guess is that you copied the files onto an external hard drive which
was formatted for Windows (with vfat). If you tried to read the images from the
same drive can confuse Linux systems, because Linux is literate, whereas vfat
does not distinguish between capital and lower
Hi Gerard Pavel
Isn't this the proviso I was referring to, that one cannot in practice
use an infinite weight because of rounding errors in the target
function. The weight just has to be 'big enough' such that the
restraint residual becomes sufficiently small that it's no longer
significant.
We are searching for outstanding postdoctoral candidates that wish to pursue
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Hi Folks,
Sorry for the pre-xtallo question; pre-xtallo right now, but hoping to
take my protein the xtallo way one of these days!
I am currently performing Thermofluor assays with my protein and the
results show that the Tm is ~45C. I am looking for some examples of
proteins and their
There is a nice paper
Comput Biol Chem. 2009 Dec;33(6):445-50. Epub 2009 Oct 20.
Predicting melting temperature directly from protein sequences.
Ku T, Lu P, Chan C, Wang T, Lai S, Lyu P, Hsiao N.
They have a list of 35 different proteins with their Tms with the references
from where they
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Due to some recent changes in both funding and personnel, I have several
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Dear All
one thing I remembered from what Gerard pointed out was the difference
in the XPLOR/CNS formalism between strict and restrained which is not a
continuum. Restrained was obviously when you had multiple copies and they were
restrained with a weight (which was like a force
Not sure whether this is the kind of information you are looking for:
The protein with PDB-ID 1ofc had a melting temperature of 37deg (from CD), which
was supported by the fact that it did not express in E.coli at that temperature.
At 20deg it expressed to about 60mg / (liter LB), could be
Hello -
The excellent paper of McCrary, uses differential scanning
calorimetry, which will give an absolute measure of thermostability.
Using Thermofluor I would be afraid you can only assess the relative
thermostability of one protein in different conditions.
As your fluorescence reporter
Dear All,
first I want to thank all of you who kindly have sent me corrections,
suggestions, and updates to BMC. Very helpful and much appreciated.
In preparation for the e-book version and for the next printing, these
corrections will now be incorporated by about End of October. If
anyone has
I agree that you can't take two unrelated proteins and expect their
Thermofluor Tms will be correlated with CD/DSC values. We've done quite
a bit with point mutants, and it works well for that (see an example in
our paper below). Also note that the dye is a perturbant the reduces
the
Maybe there is a domain shift of your protein compared to the model. If this
is the case, try to do the MP with successive domains.
2010/9/13 Paul Holland pholl...@umd.edu
Hello fellow crystallographers,
I am trying molecular replacement for a protein crystal dataset that has
very high
I think you could answer this by performing the following thought experiment:
1. Refine the structure to convergence using strict NCS constraints.
2. Switch to using the equivalent 'infinite-in-the-limit weight'
restraints, keeping everything else as is continue refinement of the
output from
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