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Dear Obayed,
it is not clear to me whether with 'nothing is working' you mean to
concentrate the solution even further or whether you mean that you do
not get crystals from 7mg/ml.
If you refer to the former, I would proceed with crystallisation
Here's an alpha release of my nucleic acid model building program for
the early adopters among you to try out. There's no GUI, there's only a
Linux binary for now, the features are rather limited, and it's only
been tested on synthetic data. On the other hand, it seems to work for me.
Re Neutron Data Collection:
1. What are the limits to data set completeness imposed by a Laue experiment
versus those of monochromatic data collection?
2. What problems are caused by flash freezing the larger protein crystals used
for neutron data collection which do not occur for X-ray data
As I know, you have 3 choices:
1, You can apply a free educational-use-only MacPymol from the
company, Schrodinger,
LLC. This is the easiest way, just move the MacPymol program into your
Program Folder.
2, I think you still can try to install Pymol by Fink. Just follow the wiki
page of
On Sep 21, 2011, at 14:57 , Xiaoguang Xue wrote:
And It is impossible to install MacPorts and Fink at the same time.
...not at all! We have both Fink and MacPorts installed on our machines (in /sw
and /opt/local, respectively), and they happily coexist.
HTH, Luca
Luca,
Thanks for your correction!
Best wishes!
Xiaoguang
On Sep 21, 2011, at 9:05 PM, Luca Jovine luca.jov...@ki.se wrote:
On Sep 21, 2011, at 14:57 , Xiaoguang Xue wrote:
And It is impossible to install MacPorts and Fink at the same time.
...not at all! We have both Fink and MacPorts
For a fourth choice, you can do a stand-alone build of PyMOL and its
dependencies with relatively little problem (at least on 10.6; haven't
upgraded yet).
Pete
Xiaoguang Xue wrote:
As I know, you have 3 choices:
1, You can apply a free educational-use-only MacPymol from the company,
Hello All,
I apologize in advance for the off topic subject but does anyone out there have
access to a journal called Anticancer Agents Med Chem ? I am having difficulty
obtaining this article: http://www.ncbi.nlm.nih.gov/pubmed/21707505 and I would
really like to have a look at it. Thanks for
Choice #5: you can purchase a licensed version?
Petri
On Sep 21, 2011, at 4:38 PM, Pete Meyer wrote:
For a fourth choice, you can do a stand-alone build of PyMOL and its
dependencies with relatively little problem (at least on 10.6; haven't
upgraded yet).
Pete
Xiaoguang Xue wrote:
Hi all,
I've been trying to crystallize a 3 protein complex recently with little
success. However, crystals of each subunit have previously been crystallized. I
was wondering if any one knows of any literature/experiences where people have
used seeds from an individual subunit to seed for a
On Wed, 2011-09-21 at 18:04 +0100, Peter Hsu wrote:
Or is this just a crazy/bad idea?
If there is one thing that I learned about crystallization, is that very
few ideas are so crazy that they are bad (i.e. not worth trying). Well,
if dried seaweed and ground horse hair are good for seeding, I
I forgot to mention, I can reconstitute the complex (co-expression/mixing
proteins) and the complex comes off both ion exchange and an SD200 as one peak.
Just haven't had luck with getting crystals.
Rex,
There are people more qualified to answer your question 1 than I am, so I am
going to politely defer that answer. The answer depends on the unit cell
dimensions, detector distance etc, and yes, there are more observations
rejected due to overlap than would be the case in monochromatic
The idea is not at all crazy. In a sense it is quite similar to
Stoichiometric variation screening* if you consider that the lattice of
the crystallized subunit may contain planes
that might be conserved in the crystal of your hope for 3 protein complex.
*Stura, E.A., Graille, M., Taussig,
Hello Dr. Palmer-
There may be other representatives in the literature by now but the one
study I know of that examines the usefulness and limitations of determining
cryo-neutron structures is The 15-K neutron structure of saccharide-free
concanavalin A, Blakeley et al. (2004), PNAS,
Experimental Postdoctoral Position in High Throughput Small Molecule Ligand
Screening
Outstanding postdoctoral applicants to work jointly with Drs. Julia Kubakek,
Mark Hay and Jeffrey Skolnick at the Georgia Institute of Technology are sought
with the following qualifications:
* Extensive
Dear Rex,
1. What are the limits to data set completeness imposed by a Laue experiment
versus those of monochromatic data collection?
Laue allows for a greater number of Bragg reflections to be measured compared
to monochromatic data collection over a give time period. The limiting factor
in
agree, any crystallisation idea is worth pursuing, given you have or can make
enough sample to try it with.
having said that, wouldn't you tend to select for the same crystals as the
seed, i.e. crystals of the component on its own?
have you tried limited proteolysis of your sample, incl. a
Hi Tim
Thanks for your mail. Both are true. I have not got crystals yet. I have tired
different truncated constructs as well as concentration for crystallization.
Even i set up the tray at 2 mg/ml but still proteins are not mixing well with
the drop solutions rather sitting on the middle of
Dear all,
I am wondering if anybody did NCS average for Anomalous map. Based on
my knowledge, there are two days to do it.
1, Use Map average in CCP4 program (input from map which cover unit
cell, create averaged density for whole unite cell )
2, Use NCS map in coot program.
However, I got
Why not ask the authors for a reprint?
JPK
On Wed, Sep 21, 2011 at 10:49 AM, anna delprato del_...@yahoo.com wrote:
Hello All,
I apologize in advance for the off topic subject but does anyone out there
have access to a journal called Anticancer Agents Med Chem ? I am having
difficulty
Hui/Phoenix,
It is pretty hard to say from what you describe which method is right.
The NCS maps in coot will give you a correct - but not as good of an
estimate of your density - if, and only if, you have enough of a model
and you have defined your NCS master and slave chains correctly. If
you
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