We are working with a multi-domain protein crystallized in SG P6_5 with
one molecule per asymmetric unit. The structure was refined at 2.00 A
resolution with reasonable R-factors but unfortunately the domain we are
most interested in seems to be disordered. Interestingly, the
self-rotation function shows peaks on the kappa=180° plane (omega=90°,
phi=19° (and every 30°)), with more than 50% origin peak height.
Therefore, we are wondering if perhaps the space group assignment might
be sub-optimal. Any explanations how these self-rotation peaks could
occur and how we could extract meaningful information to resolve the
disordered domain are welcome.
Best regards,
Peer
P.S. Some additional information: pointless suggests SG P6_5, the data
doesn't seem to be twinned (L-test), the refined part of the structure
has no "internal symmetry" and refinement in P1 doesn't reveal the
"lost" domain.
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Peer Mittl, PD Dr.
Biochemisches Institut
Universität Zürich
Room 44M03
Winterthurer Strasse 190
CH-8057 Zürich
Tel. +41-(0)44-6356559
Mobile +41-(0)76-2776566
Fax. +41-(0)44-6356834
Mail mi...@bioc.uzh.ch
