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Dear all,
the FCCC license for the program scwrl4
(http://dunbrack.fccc.edu/scwrl4/license/index.html) says that
"Licensee will take all reasonable precautions to avoid any
unauthorized disclosure of SCWRL4.0."
I may misunderstand the meaning of the
Tim, doesn't para 12 of the Agreement cover that:
"If SCWRL4.0 is installed on computers owned by a corporation or other
legal entity, then this agreement is formed by and between FCCC and
such entity ("Licensee"). You represent and warrant to FCCC that you
have the authority to bind Licensee to t
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Dear Ian,
it depends whether George Sheldrick's group can be considered a 'legal
entity', or whether the next available legal entity would be the
Inorganic Chemistry Dpt. - in the latter case I would not think I have
the authority to bind the Dpt. to
Sorry for the off-topic post…
Does anyone know of software that predicts the membrane-association domain of
peripheral membrane proteins using sequence and/or atomic coordinates?
Thanks.
John J. Tanner
Professor of Chemistry and Biochemistry
University of Missouri-Columbia
125 Chemistry Buildi
Dear Collegues,
Does anybody know how to use the server http://checkcif.iucr.org/? I have
downloaded structure factor and structure model cif files of a structure
from PDB. However it looks this server only accept one single file, it does
not work if these two files are uploaded separately. My ques
Hi,
The interface for uploading both structure factor and model files can be
found here:
http://journals.iucr.org/services/cif/checking/checkfull.html
Checkcif is mainly intended for checking the structural details of small
molecule CIF files - I have no idea what it will make of mmcif-format PD
On 15 août 2012, at 02:23, Wataru Kagawa wrote:
> Hi Jinyi,
>
> Do you have two versions of python installed?
> Maybe executing "fink remove python" will solve the problem (?)
Hi,
After updating to Mountain Lion, coot crashed when launched from the phenix
GUI. But launching coot from the term
Dear all
I made deletion mutation of a stretch of 20 amino acids on my protein. I can
purify and crystallize wild type protein but not the mutated. Mass spec on gel
separated protein shows degradation of mutant losing about another 150 amino
acids. Is there any way of purifying this non-stable
Hi Theresa,
The deletion probably led to a folding problem, making it susceptible to
residual proteases. You might try the following:
-Lysis and purification in the presence of 1mM EDTA, which can help to
neutralize proteases in addition to the protease inhibitor, without significant
leaching
In addition I would try expressing very late and short.
Growing up your cells to the maximum OD600 and then inducing for as short as
you can at lower temperature e.g. 16-20 ˚C
Your protein might be degraded while expressed.
Jürgen
On Aug 21, 2012, at 4:28 PM, Das, Debanu wrote:
Hi Theresa,
The
Need more information:
1. Do you actually know the smaller protein is actually your target
protein, or is it an impurity protein present in host cells? It
could be that your truncation simply does not express well, and the
darkest band in your crude lysate is something else.
2. Are you d
On 21/08/12 19:02, Niu Tou wrote:
Does anybody know how to use the server http://checkcif.iucr.org/? I
have downloaded structure factor and structure model cif files of a
structure from PDB. However it looks this server only accept one
single file, it does not work if these two files are uplo
In addition to the other very good suggestions, you could consider
using a purification tag at both the N- and C-termini of your protein
to only pull out full length protein. I've had success with Flag+His
and MBP+His.
Ho
Ho Leung Ng
University of Hawaii at Manoa
Assistant Professor, Department
Hi,everyone,
Does anyone here could recommend such a database for me? I've searched
the web and only find tools like 'consurf'. Databases like 'consurf' are
important for the analysis of the current known structures. However, for
the original discoveries of new domains, sequence databases with s
Dear Yuan Shang,
HSSP provides multiple sequence alignments with conservation scores per
position. It is originally PDB derived in the sense that a multiple sequence
alignment already exists for each PDB entry. You can also make HSSP entries
from sequence alone, but you should contact the HSSP m
Dear Theresa,
You could try to add 50 mM of L-Arg and 50mM L-Glu to your buffers during
purification. These amino acids are effective in preventing protein aggregation
and precipitation and protect samples from proteolytic degradation.
Cheers,
Arnaud
On Aug 21, 2012, at 10:15 PM, Theresa Hsu
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