you can try the following link:
http://pic.mbu.iisc.ernet.in/
Seema Nath
Dear Appu,
I am not sure that I have a complete sense of the issue at hand since some
of the information needed to think your issue through is missing in your
email. For example, to what high resolution cut-off were the data measured?
What resolution limits were used for the MR search? How do the
Dear members,
I am doing a molecular replacement of a
transcription factor whose ligand binding structure(24000 Da) is available
in PDB but not for the DNA binding(13000 Da). When i am searching for the
two copies from ligand binding domain as a template model, i am getti
Try PDBSum
Jürgen
On Mar 23, 2013, at 9:34 AM, Faisal Tarique wrote:
Dear all
I am working on a thermostable protein and i have read that the stability to
high temperature is due to various ionic interactions among the amino acid
residues of the protein itself..I request you all to tell me an
George, would you please explain your comments? We've found the TA
Instruments analysis software very robust and user friendly.
We have the low volume nanoITC from TA instruments and get equivalent #'s
in our comparison tests to the Microcal instrument.
Cheers,
Chris
--
Christopher L. Colbert
On 03/23/2013 09:59 AM, Wei Feng wrote:
Can you help me to check out why these maps can not be converted by
sftools?
sftools is not for manipulating map files. Mapman from uppsala software
factory would be a good choice. xdlmapman, a gui frontend to it, used
to be part of ccp4.
--
Oh, sudde
Keep in mind that output files from nanoITC, TA instrument cannot be red by
Origin. At some point you will need to analyse your data further.
George
-Original Message-
From: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] On Behalf Of
Anastassis Perrakis
Sent: Saturday, March 23, 20
Dear Chen
you can use the Matrix Copy command in pymol to align maps. Check the pymol
wiki for details and an example how to use:
http://pymolwiki.org/index.php/Matrix_copy.
Best regards
Florian
Date:Thu, 21 Mar 2013 23:29:31 -0400
From:Chen Zhao
Subject: Map Alignment
Dear all,
D
Dear all
I am working on a thermostable protein and i have read that the stability
to high temperature is due to various ionic interactions among the amino
acid residues of the protein itself..I request you all to tell me any web
server which can show all the ionic interactions between amino acid
Dear colleagues,
We are planning to replace our crystallisation hotel, a CrystalPro system that
has already done its job. We are undecided about what new system to choose and
would much appreciate hearing your experiences with your own systems.
We are looking for a unit with a capacity of
It might be worth to consider the question more in detail.
Do you want to study thermodynamics of the interaction, or a KD would do? If
the former, you need ITC. If the latter, and you want to study things at the
level of KD only, maybe investing on a plate reader, thermophoresis, or some
biose
A 2-years postdoctoral research position is available at the
Structural Glycobiology Group, Unit of Biophysics (UBF), The Basque
Country, Spain. The UBF is a research center located nearly Bilbao,
and is equipped with state-of-the-art research facilities including
X-ray protein crystallography and
I would recommend the Microcal ITC 200, hands down. Not only is it an amazing
instrument with the optional automated sample loader (which is worth every
penny), but we were able to do experiments (multiple) using FULL-LENGTH p53
binding to a weak cognate protein. I believe this was the first tim
Dear All,
I am sorry for the off topic question. I am going to buy ITC to study
protein-protein & protein-ligand interactions
I am comparing microcal, GE and nanoITC, TA instrument..
any suggestions, recommendations, good experiences or bad experiences. is
there a better system.
Thank in a
14 matches
Mail list logo
