Dear All,
just writting due to one problem concering the 'image diffraction
library'. I just build some code for some xds automatisation and would
like to use the 'image diffraction library' for the readout of the image
header informations.
The problem I ran into is the output of the ".getTw
On behalf of Michael Rossmann:
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Applicants should have experience in computer program development or
adaptation for crystallography or electron microscopy. Please e-mail
applications to Michael Rossmann, [EMAIL PROTECTED] (D
Hi,
I am working on an acidic protein with a pI value around 4.5. Although I can
obtain proteins with decent solubility, I haven't been able obtain crystals. I
was wondering if anyone would have some suggestions to increase the chances for
crystallization.
Thanks,
Erkan
Tryptic digest of the excised gel band, followed by rigorous peptide
matching helped us identify a fragment in a very recent case. The
crystallographic results confirmed MS findings.
Curiously, the ends were 'ragged' so direct ESI-MS was not very useful,
likewise the N-terminal sequencing would no
Hi Jeff,
I have seen this error before (with only DNA) when I had made mistakes
in the chain selection (segids) in dna_rna-restreints.def.
Best regards,
christian
J Knight wrote:
Hello,
Im working on a DNA, RNA, and protein ternary complex. Im having some trouble
with refining using CNS an
Hello,
Im working on a DNA, RNA, and protein ternary complex. Im having some trouble
with refining using CNS and MR. When trying to restrain a DNA-RNA base pair, I
recieve the following message and:
%PLANe error encountered: Fewer than 4 atoms selected!
CNS aborts following this message. I do
ESI-MS at a precision of +-2 Da should work alone.
Best wishes
Kornelius
On Tue, 1 Jul 2008 19:32:56 +0100
Matthew Chu <[EMAIL PROTECTED]> wrote:
> N-terminal sequencing / MS for intact mass analysis are the only ways that I
> can think of.
>
> Matt
>
> 2008/7/1 Klaus Futterer <[EMAIL PRO
N-terminal sequencing / MS for intact mass analysis are the only ways that I
can think of.
Matt
2008/7/1 Klaus Futterer <[EMAIL PROTECTED]>:
> We have a 150 kDa protein that reproducibly crystallises at one of the
> Hampton Screen conditions. However, we know from SDS gel analysis that the
>
After years of service and hundreds of structures we here at ALS 8.3.1
have finally replaced our ADSC Quantum 210 detector with a bigger Qantum
315r. I admit it is nice having the bigger detector, but now I need to
find a good home for our old workhorse. We have been through a lot
together, a
It's odd because coot gives flat riboses even if you remove all the
torsion info from the dictionary
Phil
On 1 Jul 2008, at 15:31, Jim Naismith wrote:
I don't know how many of you are frustrated with AO5* in NADP NAP
(and in
NAD). I trolled the web looking for a solution but did not find it
I don't know how many of you are frustrated with AO5* in NADP NAP (and in
NAD). I trolled the web looking for a solution but did not find it.
I think I have converted the current NAP nomenclature from the EBI in REFMAC
and COOT to use the new agreed nomenclature for this residue. Simply replace
yo
dear CCP4BB Mailing list
I sent the message copied below to the mailing list
yesterday, but since it was my first attempt to post a message, it
may not have gone through. Here it is again. Please pass along the
information to any of your colleagues who may not be on the CCP4BB
Mailing list.
Subbu,
Take a look at the following for an example of how to proceed.
J. Ay et al., Proc. Natl. Acad. Sci. USAVol. 95, pp. 6613–6618, June
1998 Structure and function of the Bacillus hybrid enzyme GluXyn-1:
Native-like jellyroll fold preserved after insertion of autonomous
globular domain
Hi :
Very interesting question that you are pointing out !. I have no
experience with enzyme chimeras, however I think that if you got crystals
and they diffract you should be able to solve the structure by MR using
one or both structures as a seeding model within the chimera.
There is a very int
We have a 150 kDa protein that reproducibly crystallises at one of
the Hampton Screen conditions. However, we know from SDS gel analysis
that the crystals contain only a 45 kDa fragment, that forms through
proteolytic cleavage over time. We would like to determine the
sequence boundaries of
Dear All:
I am working with two enzymes (40 kDa each). The crystal structures of
the two enzymes are known.
I have made a hybrid enzyme of the two individual ones.
This chimeric/hybrid enzyme is soluble and exhibits activity of the two
individual enzymes.
My questions are as follows:
1. Could
Continuation about this competition between crystal contacts and
"biologically-relevant contacts"
Your example is quite interesting because you were able to make the
comparison with different ligand affinities, which is exactly what we would
have like to test...
I just want to add a comment about
You could try the matrix seeding method, popularised by Allan D'Arcy et al
(Acta Cryst. (2007). D63, 550-554)
Crush up your needles, and use them to seed into a new round of screening. You
may be able to jump into a new crystal system this way
Janet
-Original Message-
From: CCP4 bulle
Hi
Anyone can help me?.
I have crystals that are needles (with twinning, apparently). The
crystalization condition is PEG 4K, 0.1 M NaAc pH 4.6 and 0.2 M ammonium
acetate. I have tried in this condition with detergents and additives and
with ligands but nothing improves the needles. Always nee
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