view article

Figure 5
Conformation of the isoalloxazine ring of the FAD cofactor in the extrapolated structure at 300 ns. Extrapolated electron-density maps, [mF_{\rm ext}^{\Delta t\_300\,{\rm ns}}]DFcalc (+3 r.m.s.d., green; −3 r.m.s.d., red), calculated between the dark and the light data set at 300 ns and phased with a model in which the isoalloxazine rings of the FAD cofactor (yellow) are either restrained to be planar (a, c) or absent (b, d). In (a) and (c) a model with a planar FAD is superimposed and in (b) and (d) the final refined light model at 300 ns is superimposed, in which the isoalloxazine bending angle is ∼10°.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Follow Acta Cryst. D
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds