More replies below (thanks all!!). Sounds like in Europe, checking in
the dry shipper is not an issue. No idea of US - I assume absence of
responses means nobody's bothering to try it, presumably too much hassle.
phx
Ed said (bb post) that airlines are meant to be happy to take dry
Hi Frank, if you really want to personally take the dewar with you, here
are my 2 cts (it is from a few years back, we send the dewars now by
fedex):
Just tossing the dewar on the check-in belt is not a good idea. It is a
roulette with ever increasing odds that the dewar will not enter the
plane
Thanks Herman. Addendum (last spam):
When flying British Airways way back, I asked to talk to safety,
explained it all to them, and they then added a note to my booking
saying that this thing was safe. So at check-in, when they asked
questions, I just pointed them to the booking, and that
(very last spam)
At a certain moment, we were flying once or twice a month, so by then I
thought they would know dewars...
It is extremely depending on the person doing the security checks but
the protocol below should get you past the most suspicious worst-case
security officers I(even in
Hi,
We regularly check in our dewars while flying between Sweden, Germany and
Switzerland.
Normally we add the IATA information regarding dry shipping dewars as well as a
letter from our department head stating that it is not dangerous, but do not
take any other precautions. It has worked
I always start MR by running chainsaw - you need a pit file or fast or
blast output with the sequence alignment of the template and your new
protein.
chainsaw will edit the template to a) renumber residues taking account of
any insertions and deletions b) prune and rename residues to the given
On Tue, 2012-04-17 at 17:49 -0400, Uma Ratu wrote:
In order to have my target .pdb, I need to mutate the residues using
coot?
Others already recommended CHAINSAW to prepare the model. Note that
coot has a nice feature under Extensions-All molecule... called [Post
MR] Fill partial residues
Ed:
Thank you very much for your advice and inputs
regards
Ros
On Wed, Apr 18, 2012 at 8:44 AM, Ed Pozharski epozh...@umaryland.eduwrote:
On Tue, 2012-04-17 at 17:49 -0400, Uma Ratu wrote:
In order to have my target .pdb, I need to mutate the residues using
coot?
Others already
Hi Theresa,
We use polymerization by incomplete primer extension (PIPE). it can use
very low (~1.5ng) of template so we don't have to use dpn1 after the
reaction.
linkhttp://www.springerlink.com/content/j02438u4434j257l/#section=92209page=1to
paper.
Brett
2012/4/17 Xun Lu xlun...@gmail.com
Dear colleagues,
We would like to bring to your attention the BANCO SANTANDER FOUNDATION –
CNIO FELLOWSHIPS FOR YOUNG RESEARCHERS TRAINED IN THE UK Programme
(deadline: May 31, 2012). This fellowship supports highly talented and
motivated young scientists who have trained in the UK and wish to
Is it safe to assume that the section headers in mol2 files are all
@TRIPOSsomething
or is all that's guaranteed the initial @?
http://tripos.com/data/support/mol2.pdf has everything TRIPOS, but that's
defining the 'Tripos Mol2 File Format' and I don't know if someone else has
defined a
Dear all
Thank you for the responses. This is summary of the replies.
Quick change method:
I believe quick change is the standard method.
I have utilized a two step method, where two portions of the gene are amplified
within the vector (instead of full vector amplification as in quickchange).
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Dear CCP4BBlers,
I was wondering how common it is that reviewers request to have a copy of the
PDB coordinate file for the review purpose. I have just been asked to supply
this by an editor after several weeks of review, after one of the reviewers
requested a copy.
Not having ever been asked
Hello,
I'm trying to figure out a way to search the entire PDB and find
proteins that have N-terminal(Calpha) to C-terminal(Calpha) through space
distances of between 10-20A. I was trying to decide if CONTACT or DISTANG
would be better to use for this, or if there is an easier way using some
Hi all,
I am working on an oxidoreductase and having some trouble during molecular
replacement.
The resolution of the crystal is 1.7 A and the space group is I4122 (a = b =
121.086, c =156.93 and alpha = beta = gamma = 90).
The cell content analysis results predicted two molecules in the
I always request both the final model and the experimental data
(assuming that they are not yet available directly from the PDB).
Obviously, this is done with assurances of confidentiality.
I don't think it's common though, since I was never asked to provide the
same by reviewers.
What exactly
36% solvent sounds too low. Most protein crystals are at ~50%. On the
other hand, if you assume one molecule, your solvent content jumps to
68% - not unheard of, but somewhat high for 1.7A resolution dataset.
But you have a good MR solution, just try to refine/rebuild and see what
you have in
One thing that Herman did not mention, is the Captain is in charge of
everything.
And these are my experiences pre-911 (~'99-'03). I was frequently flying form
Munich to New York to visit Brookhaven (sounds like a tourist).
My SOP included to figure out who the Captain on a particular flight
Dear All,
I am trying to use Arp/wArp to build an antibody-antigen complex with 1.65 A
data, there are three chains (heavy, light chains of antibody and the antigen)
in the complex, my question is how to put the sequences in the *.pir file so
that it still identifies different chains. It looks
Is your structure already searchable in the PDB ?
You might be able to send the validation report perhaps ?
How close to publication are you ?
Jürgen
On Apr 18, 2012, at 6:34 PM, Marc Kvansakul wrote:
Dear CCP4BBlers,
I was wondering how common it is that reviewers request to have a copy of
Marc,
As someone with limited experience in publishing structures but with other
experience reviewing the same I feel strongly about this. I am hoping to submit
any future papers with the pdb structure already released or submit the
coordinates as supplementary material. As a reviewer I find
Hi,
I think this practice (requesting the data) is getting more and more
common these days with some scientists having published fake
structures. You are far more protected from scientific misconduct when
you provide the data to referees (this takes place through an editorial
system - you
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