Hi all.
Apologies for the off topic, largely UK-centric posting.
In a period of fiscal uncertainty in which most governments (USA,
India, China, France, Germany) are actively increasing their
investment in R&D, the UK government is seriously considering cuts of
up to 25%, if press/analyst reports
Hi
the reason could be that refmac converts all aniso B to iso B when you do
overall B value refinement.
Without data it would be difficult to test and give definite answer.
regards
Garib
On 9 Oct 2010, at 00:15, Hailiang Zhang wrote:
> Hi,
>
> I found there are many changes between refmac_
Hi,
I found there are many changes between refmac_5.5 and refmac_5.2. For
example, the key word "REFI BREF OVER" will result in totally different
results under these 2 versions. Based on my input PDB with anisotropic B
pre-refined, refmac_5.5 gave a much higher R/Rfree than refmac_5.2. Can
somebod
I would like to thank all of you for your replies. I very much
appreciate your time and I've got some great starting points to
try out. I will put together a recap of the off- and on-board
comments in the next day or so for archive posterity.
For those looking for more details...
The protein
Hello all,
I have a structure of my protein at 1.3 Ang. There is a clear density in the
binding site but I can't seem to figure out what the ligand is. The
crystalization conditions contain PEG, sulfate, TMAO and acetate buffer. The
protein was purified by a Ni-NTA column and went into phosphate
It is just like the regular dialysis but the deserved buffer contains
charcol powder.
Meng-Chiao Joseph Ho
> How do you do this ?
> I have not heard of this, but I also never had to deal with getting rid of
> a ligand.
> However I would be interested to learn more about this method.
>
> Thanks,
>
Hi,
It could help if you said what your ligand is.
Nadir
Pr. Nadir T. Mrabet
Structural& Molecular Biochemistry
Nutrigenex - INSERM U-954
Nancy University, School of Medicine
9, Avenue de la Foret de Haye, BP 184
54505 Vandoeuvre-les-Nancy Cedex
France
Phone: +33 (0)3.83.68.32.73
Fax: +33 (0
Hi Katherine,
We had a case where we used saturating amounts of NaCl and precipitated the
protein to get rid of a very tight binding ligand (Structure, 11, 677-690,
2003; look at the "preparation of the apoenzyme" section).
Regards,
Mathews
-Original Message-
From: CCP4 bulletin boar
We often dialysis protein against charcoal to remove small molecules that
tightly bind to protein.
Meng-Chiao Joseph Ho, PhD
Department of Biochemistry
Albert Einstein College of Medicine
> Hi all,
>
> I am working with a substrate binding protein. The protein
> scavenges its endogenous ligand out
Call for applications to the Membrane Protein Lab at Diamond
Dear Crystallographers,
The Membrane Protein Laboratory (MPL) at Diamond Light Source in
Oxfordshire (UK) is pleased to announce that is now open our call for
proposals.
The MPL is a joint venture between the Diamond Ligh
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