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![[Figure 6]](rr5179fig6mag.jpg)
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Figure 6
Expression and purification of AtRLPs. (a) Schematic representation of different RLP expression constructs. Variations include different signal peptides (DmBIP, signal peptide from D. melanogaster binding protein; AtNat, native A. thaliana signal peptide, GP67, baculoviral glycoprotein 67 signal peptide, SRF6 N-cap, utilization of the whole SRF6 N-terminal capping domain) and variable construct lengths (including or omitting the charged C-terminal tail). (b) Example analytical size-exclusion chromatography traces from RLP purifications. A peak for a monomeric, neither aggregated nor degraded RLP ectodomain (MW of ∼100 kDa) would be expected at an elution volume of ∼13 ml (indicated by an arrow). The void volume (v0), the total column volume (vt) and the elution volumes for molecular-mass standards (Al, aldolase, 158 kDa; Co, conalbumin, 75 kDa; Ov, ovalbumin, 43 kDa; CA, carbonic anhydrase, 29 kDa) are indicated. (c) Example analytical size-exclusion chromatography traces for AtRLP23 purifications from co-expression with SOBIR1–283 alone (blue), with the RLP23 ligand PpNLP20 and the co-receptor AtSERK1 (grey), and with SOBIR1, SERK1 and the ligand PpNLP20 (brown). Labels are as in (b). |
![[Figure 6]](rr5179fig6.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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