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Does anyone know of crystallization conditions for proteins that are
easy to make (or better, purchase) and that reliably give merohedral
twinning. I'd like to do some more systematic crystallization
experiments to understand what triggers the lattice discontinuity and of
course find ways to prevent it.
Bart
[EMAIL PROTECTED] wrote:
For what it's worth, I have a near-perfect merohedral twin (~ 40%
contribution from twin domain to diffraction) that I have only
observed from one very large crystal (1.8 x 1.0 x 0.4 mm) grown in
microbatch under parafin oil. Smaller crystals grown by hanging or
sitting drop in smaller volume set-ups do not seem to have this
phenomenon. Most all the other variables are the same for these
crystals, such as protein [], reservior solution, temperature,
purification procedure, and so on. Just the ultimate crystal volume
and growth method are different....again, for what it's worth....
Cheers
Brad
--
Brad C Bennett
Graduate Research Assistant
Department of Biochemistry, Cellular and Molecular Biology (BCMB)
University of Tennessee-Knoxville
865-974-3047
[EMAIL PROTECTED]
-------------- Original message from Stefano Benini
<[EMAIL PROTECTED]>: --------------
> *** For details on how to be removed from this list visit the ***
> *** CCP4 home page http://www.ccp4.ac.uk ***
>
>
>
> Dear crystallisators,
>
> I would like to know what people usually tries (possibly
succesfully!)
> to get not twinned crystals when a protein tends to crystallise
as a
> perfect twin
>
> I am trying/plannning to try: finding new conditions, additives,
> detergents, tag removed, new construct, etc.,
>
> Thank you very much
>
> Ciao
> Stefano
>
> **********************************
> Stefano Benini Ph.D.
> http://www.ysbl.york.ac.uk/~benini
> York Structural Biology Laboratory
> University of York
> Heslington
> York YO10 5YW United Kingdom
> Tel.:+44 1904 328276
> Fax: +44 1904 328266
> "verba volant scripta manent"
> **********************************
>
>
