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]
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]>: --------------
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>
>
> 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"
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