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. Author manuscript; available in PMC: 2018 Sep 5.
Published in final edited form as: Structure. 2017 Jul 27;25(9):1325–1336.e3. doi: 10.1016/j.str.2017.06.016

Table 1.

X-ray Data Collection and Refinement Statistics

Construct FGF9-FGFR1c
Data Collection
X-ray wavelength 0.97900
Space group P212121
Unit Cell Dimensions
 a, b, c (Å) 42.159,86.793,136.857
 α, β, γ (°) 90.00,90.00,90.00
Resolution (Å) 50–2.50(2.54–2.50)a
No. measured reflections 114188
No. unique reflections 18063(867)
Data redundancy 6.3(6.1)
Data completeness (%) 99.4(97.6)
Rsym (%)b 8.7(37.8)
I/sig 29.8(4.0)

Refinement
Resolution (Å) 29.5–2.50(2.57–2.50)
No. unique reflections 18002(1330)
No. Reflections (Rfree)c 1799(133)
Rwork/Rfree 18.26/22.82(21.82/29.73)
No. atoms
 Protein 2764
 Ligand/Ion 15
 Solvent 58
R.m.s. deviations
 Bond length (Å) 0.009
 Bond angle (°) 1.208
Average Bfactors (Å2)
 Protein 52.25
 Ligand/Ion 126.63
 Solvent 44.04
Ramachandran Plot
 Outliers (%) 0.00
 Allowed (%) 4.46
 Favored (%) 95.54
Rotamer outliers (%) 1.68
No. C-Beta Deviations 0
All-Atom Clashscore 5.27

PDB ID 5W59
a

Values in parenthesis are for the highest resolution shell.

b

Rsym = Σ|I− < I >|/ΣI, where I is the observed intensity of a reflection, and <I> is the average intensity of all the symmetry related reflections.

c

Number of reflections randomly excluded from the refinement for Rfree calculation.