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. Author manuscript; available in PMC: 2013 Oct 4.
Published in final edited form as: Nature. 2013 Mar 17;496(7443):64–68. doi: 10.1038/nature11964

Figure 1. Structure of mCRY2-PHR in apo- and FAD-bound forms.

Figure 1

a, Overall structure of the apo mCRY2-PHR domain. b, mCRY2-PHR-induced quenching of FAD fluorescence. Inset shows FAD fluorescence quenching with mCRY2-PHR concentration titrated (error bars representing s.d.). c, A close-up view of FAD bound to mCRY2-PHR with positive Fo − Fc electron density contoured at 1.5 σ and calculated before the cofactor was built (green mesh). d, mCRY2-PHR and Drosophila (6-4)-photolyase are superimposed with their FAD cofactors shown in sticks and their FAD carbon atoms colored in yellow and green, respectively.