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. Author manuscript; available in PMC: 2021 Dec 7.
Published in final edited form as: Cell Rep. 2021 Oct 19;37(3):109834. doi: 10.1016/j.celrep.2021.109834

TABLE 1.

Crystallization Conditions, Data Collection, and Refinement Statistics

Protein sNrk/s-dRor2 sDrl-2
PBD ID 7ME4 7ME5
Crystallization Conditions 3 mg/ml protein, 50 mM Bis-Tris propane (pH 5.0), 20% PEG 3350, 21°C 12 mg/ml protein, 100 mM Tris (pH 8.5), 100 mM sodium acetate, 25% PEG 6000, 15% glycerol, 21°C
Data Collection a
Source APS 24-ID-E Rigaku 007HF
Wavelength (Å) 0.9792 1.5418
Space Group C2 C2221
Cell Dimensions
 a, b, c (Å) 95.70, 74.69, 61.55 56.97, 91.58, 76.36
 α, β, γ (°) 90, 106.31, 90 90, 90, 90
Resolution (Å) 45.61 – 1.75 50.00 – 2.0
Completeness (%) 88.5 (78.0) 99.53 (94.2)
Redundancy 2.2 (1.8) 6.6 (3.6)
Rsym 0.046 (0.744) 0.061 (0.769)
I/σ 9.1 (1.0) 19.1 (1.5)
CC1/2 0.998 (0.630) 0.999 (0.597)
Refinement
Number of reflections 36,909 13,749
Rwork/Rfree (%) 19.9/22.2 21.8/24.8
Number of atoms
 Protein 1,833 1,209
 Ligands 18 -
 Carbohydrate 28 14
 Water 275 84
Average B factor (Å)
 Protein 41.95 25.26
 Ligands 75.53 -
 Carbohydrates 63.49 90.50
 Water 49.26 52.30
Ramachandran favored (%) 97.7 99.3
Ramachandran allowed (%) 2.3 0.7
Ramachandran outliers (%) 0 0
Bond length rmsd (Å) 0.009 0.006
Bond angle rmsd (Å) 0.950 0.784

Numbers in parentheses denote highest resolution shell