Extended Data Fig. 2: Crystallization of ΔCRD-FZD4 and structure determination. | Nature

Extended Data Fig. 2: Crystallization of ΔCRD-FZD4 and structure determination.

From: Crystal structure of the Frizzled 4 receptor in a ligand-free state

Extended Data Fig. 2

a, Schematic of the ΔCRD-FZD4 construct. To obtain crystals that would diffract well, we truncated the N-terminal CRD region (residues 1–177) and C-terminal flexible region (residues 517–537) and introduced four single mutations (M309L, C450I, C507F and S508Y, coloured in red) that are designed based on sequence conservation analysis across ten human FZDs. Residues that are involved in the X.50f numbering system are coloured in green. The cysteines that form endogenous disulfide bonds are indicated in orange. b, Fluorescence-activated cell sorting staining data, to monitor the surface expression of the construct used in this study. The experiment was repeated twice with similar results. c, Crystals of ΔCRD-FZD4 in the apo state. d, Crystal packing of ΔCRD-FZD4.

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