Hi,
I am trying to process data with the new XDS version (June 2nd)
however the new space group determination sub-routine is picking the
wrong space group. Can I simply run CORRECT after the INTEGRATE step
as in the old version putting in the space group I want? If so is
there no longer
Hi James,
Derek Logan wrote:
- When Rontgen discovered a new kind of light, he called it
x-rays. Now only the Germans call them Rontgen rays.
Thanks for a great essay! Since I have nothing of real value
contribute here, I won't pass over the opportunity to be a
besserwisser (as the Swedes
Hi Sam,
The effect of reducing agents like beta-ME, DTT or TCEP is exactly as you say,
the prevention of disulphide formation or cleavage of existing disulphide
bridges and therefore prevention of aggregation if inter-molecular disulphide
bridges can be formed.
A balancing of reducing power, or
I hope this isn't too much of a foray into philosophy and semantics,
but can't you argue that the crystals themselves are weak complexes?
And since the energies of crystal contacts are typically very weak, I
would further argue that you should be able to crystallize ANY
complex with an
The word weak is, of course, relative. Free energy of crystallization
is roughly 1-2 kcal/mole of crystal contacts (I think I carried this
number from Sir Blundell's book, but quick look at papers by Peter
Vekilov's group seems to confirm it - am I wrong on this?). I think
that crystal contacts
Another question re: Amicon stirred cells...
I also seem to recall seeing 1L size stirred cells in older labs of my
youth. My current lab has acquired one of 400 mL, but looking to
purchase a bigger one, I can't find any. Any ideas about where we might
find one?
Evette S. Radisky, Ph.D.
Hi Gina,
From a lab near you ... gd resolvase without DNA: a
hexagonal crystal form can be grown from either the
catalytic domain only (missing the DNA binding domain, ~1/3
of the protein) or the intact protein. The binding domain
is there when you run crystals down a gel, but disordered
Hi there
I actually just consulted, about your question, with one of the
longer term members of the department about this. And we came to the
conclusion that 4- 500ml was probably the maximum size.
Gina
On Jun 30, 2008, at 11:15 AM, Radisky, Evette S., Ph.D. wrote:
Another question re:
There are quite a number of structures homodimers and homotetramers in the PDB
where the dissociation constant is known to be in the millimolar range.
For example the dimerizaion of a humainized antibody VHH domain that mimicks a
VH-VL complex (Conrath et al. J. Mol. Biol. (2005) 350, 112125).
Hi,
There might be newer articles on this topic, but I found this review helpful,
http://www.nature.com/nrm/journal/v6/n3/abs/nrm1589.html;jsessionid=0F74B47AB573CDBCD1D5BC5941C01B9F
Kianoush
--- On Sat, 6/28/08, Gina Clayton [EMAIL PROTECTED] wrote:
From: Gina Clayton [EMAIL PROTECTED]
Evette,
A good machine shop can make a 1 L Amicon-like tirred-cell
concentrator quite easily (and many have). But another alternative
is the Pellicon Tangential Flow Filtration Cassettes (see http://
www.millipore.com/techpublications/tech1/pb022). The Pellicon XL 50
cassettes (50 sq.
Dear colleagues,
I am trying to find a cuvette for Dynapro 99-CP. Wyatt does not seem to
have these cuvettes. If anyone knows where I can get one please let me
know.
Thanks.
Jackie Vitali
Four examples of disordered domains in crystal structures:
Disordered domains of calmodulin
Wilson MA, Brunger AT.
Domain flexibility in the 1.75 A resolution structure of Pb2+-calmodulin.
Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1782-92. Epub 2003
Sep 19.
PMID: 14501118 [PubMed
Hi,
we've had a similar situation: a protein-peptide complex with a Kd in the
nM range crystallized in the same condition as the protein alone, and
yielded a structure of a complex (voltage-gated calcium channel beta
subunit). The exact crystal contacts turned out to be a bit different, as
the
Dear all,
I'm am trying to refine an isopeptide link in diubiquitin between a
Lys side chain and a Gly 76 C-termini. The link has reasonable
geometry (planar amide bond) prior to refinement with refmac
5.2.0019. After refinement, the peptide link is no longer planar.
Any ideas how to
Dear Gina,
We have recently solved a structure of the glucosamine 6P synthase from E.coli
(GlmS) and surpringsly, although the whole protein was present in this crystal
form, no electron density was observed for the glutaminase domain (240 residues
out of 600), indicating its mobility.
Dear Filip and others,
To play Devils advocate, this could also (in the absence of strongly
supportive biochemical data) be interpreted as a crystal artifact, with the
weakly binding ligand not forming a physiologically relevant contact but
merely occupying the - haphazardly - empty space in
Dear Jens,
There is an overwhelming amount of evidence that our mutants still binds to
the same site in solution and in vivo - there is a correlation between
decrease in binding affinity (calorimetric measurements) and
function (electrophysiological measurements) for more than 20 mutants based
on
Hello John,
No, they're not. Crystals were obtained at pH8.0, 200mM NaCl; 10%
PEG4000. Calorimetric experiments were done at pH7.4, 150mM KCl. We found
the interaction to be driven mainly by hydrophobic contacts (mutants of
polar/charged residues have no significant effect on the affinity).
Thank you very much for your programme.
But when I use this specific chainsaw to repeat a successful example on my
computer, I see a new error log as following chainsaw: error while loading
shared libraries: liblapack.so.3: cannot open shared object file: No such file
or directory. I cann't fix
20 matches
Mail list logo
