Le 11 nov. 09 à 14:26, Jürgen Bosch a écrit :
> Dear CCP4 community,
> (hijacking the thread)
> I so far failed to get a sulfur SAD phased structure and I blamed it
> on the low symmetry space group C2 plus weakish diffraction if you
> don't want to overexpose your crystal and be able to collect 20-30x
> redundancy.
> What do the expert think about fine slicing versus "regular" data
> collection for sulfur SAD phasing ?
>
> Thanks,
>
> Jürgen
Hi Jürgen,
You may find this paper interesting:
Lakomek, K., Dickmanns, A., Mueller, U., Kollmann, K., Deuschl, F.,
Berndt, A., Lubke, T., and Ficner, R. (2009) De novo sulfur SAD
phasing of the lysosomal 66.3 kDa protein from mouse. Acta Crystallogr
D Biol Crystallogr, 65: 220–228.
It shows a case where sulfur-SAD worked for a reasonably-sized protein
crystallized in C2. There was a Xe atom, but its contribution seemed
to be negligible. No special data collection strategy is mentioned.
Best,
-- Miguel
Architecture et Fonction des Macromolécules Biologiques (UMR6098)
CNRS, Universités d'Aix-Marseille I & II
Case 932, 163 Avenue de Luminy, 13288 Marseille cedex 9, France
Tel: +33(0) 491 82 55 93
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