Figure 2.
Figure 2: Structural analysis of the human septin complex. a,
Superimposition of the molecular replacement solution using the
SEPT2 G domain onto the selenomethionine anomalous map contoured
at 5 to
assign the location of the SEPT2, SEPT6 and SEPT7 subunits in
the asymmetrical unit. b, Ribbon model of the trimeric
SEPT2–SEPT26–SEPT27 complex, with SEPT7 in cyan, SEPT6 in
pink and SEPT2 in blue, with nucleotides in ball and stick
representation. c, Positive F[o] - F[c] electron density map,
contoured at 3 ,
around the nucleotide-binding sites of the respective septins,
and the resulting nucleotide models, as indicated.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2007,
449,
311-315)
copyright 2007.
to
assign the location of the SEPT2, SEPT6 and SEPT7 subunits in
the asymmetrical unit. b, Ribbon model of the trimeric
SEPT2–SEPT26–SEPT27 complex, with SEPT7 in cyan, SEPT6 in
pink and SEPT2 in blue, with nucleotides in ball and stick
representation. c, Positive F[o] - F[c] electron density map,
contoured at 3