The Institute of Cancer Research (University of London)
Section of Structural Biology, Chelsea, London
X-RAY CRYSTALLOGRAPHY MANAGER
The Institute of Cancer Research (a College of the University of London)
is a world-class cancer research organisation. In the 2008 Higher
Education Funding
Dear Vinson,
I would agree with you on choice B. There are probably many ways to look at
it. Here are two that come to me at the moment.
1. If the reaction is reversible, then there's no opportunity to put energy
into the system to reduce its overall entropy. So a reversible epimerase would
Barring some grammatical errors, you've pretty much summed it up.
James
On May 18, 2010, at 12:31 AM, Vinson LIANG wrote:
Dear all,
Sorry for this silly biochemistory question. Thing is that I have a
reversible epimerase and I want to mutate it into an inreversible
one. However, I
Hi Francois
configure linux_intel_compilers
should do the trick. We distribute ccp4 built with the intel compilers for OS
X. Part of this is that the macs cover a much smaller range of cpus than linux
boxes, so optimisation is less of a problem. If you want speed make sure that
you are
Hi everyone,
I have two types of ligands cocrystallized with my protein, ligand 1 and ligand
2. I am only interested in resolving ligand 2. In my electron density map, only
part of ligand 1 can be identified. Is it ok for me to cut ligand 1 so only the
identifiable part is left or should I
I just checked a recent refmac job and it seems that in the output mtz
the Fobs has indeed changed. what's more interesting, the number of
missing reflections has changed too (disturbingly, it decreased so that
the dataset looks more complete 97.07% to 97.17% in this case).
But if the same
The decrease in missing reflections are due to the fact that
the output file does not include the missing reflections that
are lower resolution than the lowest resolution observed
reflection. Thus, this file is no longer uniqueified and
then refmac reports a higher completeness since it
no
Hi All,
Thanks to all that replied for the advice, suggestions etc. about my antibody.
I will definitely try the suggestions.
Christine
From: Sheemei Lok [mailto:sheeme...@yahoo.com.sg]
Sent: Monday, May 17, 2010 9:56 PM
To: Harman, Christine
Subject: Re:
On Tue, 2010-05-18 at 07:03 -0700, Miller, Mitchell D. wrote:
The decrease in missing reflections are due to the fact that
the output file does not include the missing reflections that
are lower resolution than the lowest resolution observed
reflection. Thus, this file is no longer
Hello
I am trying to complex two proteins of 57 and 18 kda and using pET 22b as an
expression system. I purified both with His tag and the purity is quite nice
after Ni-NTA (Buffer is Tris,Nacl and Imidazole). After purification with
Ni_NTA i tried to improve my protein purity using gel
For gel exclusion chromatography it is generally adsvisable to include
100 mM NaCl or equivalent ionic strength in the elution buffer to
suppress nonspecific adsorption. In addition the pH and ionic strength
of the elution buffer should be compatible with your protein folding
stability. It is
I think that it's possible to do a mutation that affects only one way of
the reaction. You can mutate a residue that makes contacts only with the
product of the direct way or only of the reverse way.
Maia
Randy Read wrote:
Dear Vinson,
I would agree with you on choice B. There are probably
You could make use of product binding energy to drive the
reaction forward while the substrate/product is bound to the
enzyme. But enzymes that pull that trick are barely
enzymes - they stay stuck to the first product they make
until something else uses some energy to release it.
You can't
POSTDOCTORAL FELLOW/RESEARCH ASSOCIATE POSITION UNIV. OF PITTSBURGH
A postdoctoral fellow/research associate position is available immediately
in the laboratory of Dr. Zhang at the University of Pittsburgh for up to 4
years funded by an NIH grant. The research project focuses on structural
Hi,
I'm more of a Fourier coefficient kind of guy, but I thought that a
ΔG of zero simply corresponded to an equilibrium constant of one. You
can certainly have reversible reactions with other equilibrium constants.
In fact I think irreversible reactions are simply ones where the
equilibrium
Vinson,
As Dale and Randy pointed out, you cannot change the ΔG of a reaction
by mutation: enzyme, which is a catalyst, affects only the activation
barrier (ΔE double-dagger). You can just make it a better (or
worse) catalyst which would allow the reaction to flow faster (or
slower)
If you change the reaction rate in one direction 1000 times slower than
in the other direction, then the reaction becomes practically
irreversible. And the system might not be at equilibrium.
Maia
R. M. Garavito wrote:
Vinson,
As Dale and Randy pointed out, you cannot change the ΔG of a
Sounds like a good explanation. Thank you.
Maia
Dale Tronrud wrote:
If you change the reaction rate in one direction 1000 times slower then
the reaction rate in the other direction will also be 1000 times slower
and the equilibrium will be in exactly the same place. You can't make
the
Dear Crystallographers,
I am trying to optimize a native gel experiment of a two-protein complex,
running the smallest-detectable amount of protein component A with varying
amounts of component B.
MWCharge MW/Charge
A 22 -5-4308
B 17-24 -702
This
Hi there CCP4ers,
I need to number a PDB file following the Kabat numbering. Is there any
script to do this numbering automatically?
Thanks a lot in advanced.
Best,
Ariel
--
*
Ariel Talavera Pérez, PhD
Nanobiology Group
Center of Molecular
Hello Everyone,
I have a reasonably well fitted electron density map through molecular
replacement. However, there is always some red region left no matter how hard I
tried when the mtz file is loaded into Coot. Is this because my model is still
not good enough or it’s natural to most model
On May 18, 2010, at 4:13 PM, Jay Pan wrote:
Hello Everyone,
I have a reasonably well fitted electron density map through
molecular replacement. However, there is always some red region left
no matter how hard I tried when the mtz file is loaded into Coot. Is
this because my model is
Dear colleagues,
whereas data sharing for most crystallographers appears to be a no-brainer,
making coordinates and (most of the time, hopefully) structure factors
available, it seems the electron microscopists are drastically lagging
behind when it comes to making data available.
Many cryoEM
When X-ray crystallographers not so many years ago thought they are the
salt of the earth, of science and then some (well, some believe so
to this date), the same attitude prevailed (data holds). Once every
person with access to Google does it, that secrecy slowly disappears.
What also
Dear Jacob, I offer you my opinion.
Are you talking about electrophoresis? As far as I know it does not work
for the mass. The velocity of a protein depends on the charge at a
particular pH, the mass and shape of molecules etc. It's very difficult
to take all these things into consideration.
Dear all,
Sorry for this silly biochemistory question. Thing is that I have a reversible
epimerase and I want to mutate it into an inreversible one. However, I have
been told that the ΔG of a reversible reaction is zero. Which direction the
reaction goes depends only on the concentration of
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