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: 220228.
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 Fax: +33(0) 491 26 67 20 e-mail: miguel.ortiz-lombar...@afmb.univ-mrs.fr Web: http://www.pangea.org/mol/spip.php?rubrique2
smime.p7s
Description: S/MIME cryptographic signature
