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![[Figure 2]](jb5072fig2mag.jpg)
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Figure 2
Crystallographic analysis of the LRR ectodomain of the Arabidopsis receptor kinase SRF6. (a) Schematic representation of SRF6 (SP, signal peptide; N-cap, N-terminal capping domain; C-cap, C-terminal capping domain; TM, transmembrane helix; JM, juxta-membrane motif). The crystallized fragment is indicated by a red line. (b) Schematic representation of a 96-well high-throughput crystallization-screen plate; conditions containing SRF6 crystals after 3 d of incubation at room temperature are shown in cyan. (c) Ribbon diagram of the SRF6 N-terminal capping domain, with Met42, Cys59, Cys68 and Met91 shown in bond representation and including a phased anomalous difference map contoured at 9σ (green mesh). (d) Overall structure of the SRF6 ectodomain. A ribbon diagram is shown; the secondary structure was assigned using DSSP (Kabsch & Sander, 1983  ). The N- and C-terminal capping domains are shown in yellow and the LRR core in blue. A disulfide bond in the N-terminal capping domain is shown in bond representation; genetic alleles previously characterized for SRF9/SUB are highlighted in magenta. (e) Example region of the SRF6 structure covering residues 50–53 and 62–64 (yellow ball-and-stick representation) and including the final (2Fo − Fc) electron-density map contoured at 1.5σ (blue mesh). (f) Structural comparison of the C-terminal capping domains in the Arabidopsis receptor kinases SERK1 (PDB entry 4lsc), SRF6 and SOBIR1 (PDB entry 6r1h). The LRR ectodomain (blue) structures of SERK1 (r.m.s.d. of ∼1.5 Å comparing 163 corresponding Cα atoms) and SOBIR1 (r.m.s.d. of ∼3.4 Å comparing 133 corresponding Cα atoms) were superimposed on the SRF6 LRR domain and presented side-by-side in ChimeraX. The C-terminal capping domains are highlighted in yellow. |
![[Figure 2]](jb5072fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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