Extended Data Fig. 10: Intra protein hydrophobic interactions of W374 in CRY2N monomer and superposition of structures of blue-light activated CRY2WT tetramer with ZmCRY1W368A tetramer and BIC2-CRY2N complex.
From: Structural insights into the photoactivation of Arabidopsis CRY2
a, CRY2N is shown in white and FAD binding cavity helices are shown in cyan. The black square shows a close-up view of residues that form intra protein hydrophobic interactions with W374. b, Superposition of structures of blue light induced AtCRY2NWT tetramer (in this study) and PHR domain of ZmCRY1W368A tetramer (PDB 6LZ3). c, Structure alignment of CRY2N tetramer (in this study) with BIC2-CRY2N complex (PDB 6K8K). Mol A and D are shown in white; Mol B and C are shown in wheat. BIC2 is shown in red. Surface and ribbon representation of BIC2 is shown. Black dashed lines indicate the clash between BIC2 and interface 2. The black square shows a close-up view of the clash with a 90° rotation.
