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Table 1 Data collection and refinement statistics

From: Crystal structure of Usutu virus envelope protein in the pre-fusion state

Data collection
 Space group P 212121
Cell dimensions
a, b, c (Å) 35.04,104.34,115.58
 α, β, γ (°) 90°,90°,90°
 Wavelength (Å) 0.9793
 Resolution (Å)a 50.0–2.0 (2.07–2.00)
 Rmergea,b 0.13 (0.808)
 I/σIa 13.51 (2.73)
 Completeness (%)a 99.6 (98.80)
 Redundancya 5.5 (4.9)
 Total reflections 161,936
 Unique reflections 29,488
Refinement
 Resolution (Å) 30.99–2.0
 Rwork/Rfreec 0.214/0.247
No. of atoms
 Protein 3111
 Water 232
B-factors
 Protein 39
 Water 42.5
r.m.s.d.
 Bond lengths (Å) 0.018
 Bond angles (°) 1.64
Ramachandran plotd
 Ramachandran favored (%) 98%
 Ramachandran allowed (%) 2%
 Ramachandran outliers (%) 0
  1. aValues for the outmost resolution shell are given in parentheses
  2. bRmerge = ΣiΣhkl | Ii-<I > | /ΣiΣhklIi, where Ii is the observed intensity and < I > is the average intensity from multiple measurements
  3. cRwork = Σ | | Fo |- | Fc | | /Σ | Fo |, where Fo and Fc are the structure-factor amplitudes from the data and the model, respectively. Rfree is the R factor for a subset (5%) of reflections that was selected prior to refinement calculations and was not included in the refinement
  4. dRamachandran plots were generated by using the program MolProbity