Statistics on data collection and phasing. Data collection values in parentheses are for the high-resolution shell.

NativeXeEMTSFYRALM peptide complexDYQRLN peptide complex
Protein construct122–435122–435122–435122–435158–435
Data collection
Resolution (Å) (outer bin)3.0 (3.16)3.0 (3.16)4.0 (4.22)2.65 (2.79)2.70 (2.85)
R merge * 0.101 (0.910)0.079 (0.851)0.116 (0.302)0.089 (0.882)0.101 (1.47)
〈〈I〉/σ(〈I〉)〉17.3 (2.9)25.9 (2.2)20.2 (7.2)21.3 (2.1)23.5 (2.2)
Completeness (%)99.9 (99.9)99.8 (99.8)99.7 (100)99.4 (96.7)98.4 (99.8)
Multiplicity10.9 (10.6)10.7 (8.2)10.4 (10.6)9.2 (8.1)15.8 (14.7)
R meas 0.106 (0.957)0.088 (0.985)0.124 (0.334)0.094 (0.942)0.104 (1.52)
Wilson plot B2)1008578
Multiple isomorphous replacement phasing
Number of sites18
R deriv 0.0960.255
Rcullis: acentric (centric)§0.643 (0.707)0.662 (0.683)
Phasing power: acentric1.88 (1.19)2.29 (1.87)
(centric)|
Anomalous phasing power0.542.28
Mean figure of merit:0.374 (0.350)0.187 (0.205)
acentric (centric)
Figure of merit after0.8640.849
solvent flattening (all data)
Refinement
R(Rfree)#0.273 (0.297)0.282 (0.325)
B〉(Å2)6075
Nreflections(Nfree)19,296 (842)18,413 (801)
Natoms(Nwater)2143 (51)2143 (50)
rmsd bond length (Å)0.0100.012
rmsd angle distance (Å)0.0380.040
  • * Rmerge = ΣΣi|Ih − Ihi |/ΣΣiIh , where Ih is the mean intensity for reflectionh.

  • Rmeas = ΣEmbedded ImageΣi|Ih Ihi |/ΣΣiIh , the multiplicity-weighted Rmerge(34).

  • Rderiv = Σ|FPHFP|/ΣFP.

  • § Rcullis= Σ∥FPHFP| − |FH(calc)∥/Σ|FPHFP|.

  • | Phasing power = 〈|F H(calc)|/phase-integrated lack of closure〉.

  • Phasing using the FYRALM complex data as native.

  • # R = Σ|FPFcalc|/ΣFP.