Extended Data Fig. 9: Dimer interface 2 and locations of CRY mutations in ZmCRY1cW368A-PHR structure. | Nature Structural & Molecular Biology

Extended Data Fig. 9: Dimer interface 2 and locations of CRY mutations in ZmCRY1cW368A-PHR structure.

From: The oligomeric structures of plant cryptochromes

Extended Data Fig. 9

a, dimer interface formed by molecules A/C (or B/D). Mol A is shown as a surface model, while C is shown as a ribbon model. FAD is depicted as yellow sticks, and the “trp-triad” residues are shown as orange spheres. b, The reported CRY mutations were located in the ZmCRY1cW368A-PHR structure. The early-flowering mutation AtCRY2V367M in the Cvi nature allele and the constitutive COP-phenotype mutation AtCRY1G380R corresponds to residues Val361 and Gly371 in ZmCRY1cW368A-PHR, respectively. Their locations near the “trp-triad”residues are shown in the structure.

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