Jacob Keller wrote:
Dear Crystallographers,
what is the dogma with regard to affinities in crystals? For example,
if I soak three crystals in 1pM, 1nM, and 1uM compound X, and they all
show equivalent density, does that mean that the affinity is really
better than 1pM, or is the crystal of such
Hey :)
Tubulin has high affinity towards colchicine. You may be able to subtract it
via colchicine-agarose if you can get some, or have some of it made.
Alternatively, merely adding colchicine may be enough to break the complex
between tubulin and whatever it is you're purifying (is it a kinase --
Dear Crystallographers,
what is the dogma with regard to affinities in crystals? For example,
if I soak three crystals in 1pM, 1nM, and 1uM compound X, and they all
show equivalent density, does that mean that the affinity is really
better than 1pM, or is the crystal of such a high local concentra
How about hydrophobic interaction chromatography?
JPK
On Fri, Jun 24, 2011 at 12:22 PM, Shiva Bhowmik wrote:
> Amonium sulfate precipitation? Considering the fact that you tried to
> seperate tubulin contamination both by charge and mass difference amonium
> sulfate pption may work.
>
> Shiva
>
Instead of an imperfect crystal, this can also occur if one chooses the
wrong Bravais lattice type (or spacegroup) to integrate. For example, if
you choose tetragonal when it is really orthorhombic with a ~ b, or if you
choose orthorhombic and beta is 90.2, then you can see that trying to force
th
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Amonium sulfate precipitation? Considering the fact that you tried to
seperate tubulin contamination both by charge and mass difference amonium
sulfate pption may work.
Shiva
On Thu, Jun 23, 2011 at 4:05 AM, Seungil Han wrote:
> All,
> I am sorry that this is off topic.
> My target protein expr
Hi Bie,
Curious to know what are the cell parameters obtained after scaling? You
mention observing perfect Chi2 statistics with lysozyme crystals. But are
you observing the same Chi2 statisctis with the crystal that yielded unusual
Y-Chi2 if you collect another dataset. If there is a consistency o
Hi Madhu,
You don't need to use scala, d*trek can do the job as well. The easiest thing
to do is to continue with d*trek to scale and merge your data and then input
this scaled and merged file into Dtrek2mtz.
Eric
Eric T. Larson, PhD
Biomolecular Structure Ce
You should also search in I212121, an
alternative space group. If you have a reasonable solution,
packing should be sensible. Matthews coefficient analysis is only
a guide, as there is a distribution of solvent content values in
typical protein crystals. We routi
Hello Marius,
not being familiar with the chromophore, but could this be done by the
prodrg-server?
http://davapc1.bioch.dundee.ac.uk/prodrg/
Tim
On Fri, Jun 24, 2011 at 12:06:54AM +0200, marius.schm...@ph.tum.de wrote:
> is there someone out there who worked out a
> cif-file WITH restraints f
On Fri, 2011-06-24 at 09:50 +0200, mullapudi edukondalu wrote:
> Dear Members,
>
> I have my first data set on one of my protein crystals, that diffract
> to 2.7 A, and the space group is I222. According to Mathews
> coefficient, there should be 4 molecules in the asymmetric unit. But,
> when I
A post-doctoral position, initially for two years, is open in the group of
Robert Gilbert at the Division of Structural Biology, Oxford
(http://www.strubi.ox.ac.uk).
We are using both X-ray crystallography and cryo-EM to determine the structures
of macromolecules and macromolecular complexes in
The preferred general route into CCP4 for unmerged data for scaling and merging
(if that is what you want to do) is through Pointless into Scala (or in future
Aimless as a Scala replacement, or the future merged Pointless/Aimless
("nameless")).
At present Pointless will accept data from Mosflm,
You do need to try space group I21 21 21 as well as these two space groups are
indistinguishable from systematic absences
Phil
On 24 Jun 2011, at 08:50, mullapudi edukondalu wrote:
> Dear Members,
>
> I have my first data set on one of my protein crystals, that diffract to
> 2.7 A, and the s
Dear Members,
I have my first data set on one of my protein crystals, that diffract to
2.7 A, and the space group is I222. According to Mathews coefficient, there
should be 4 molecules in the asymmetric unit. But, when I run molecular
replacement programme it found only 3, and the crystal packin
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