Table 4 X-ray data collection and refinement statistics for Fab CBH7

From: Cryo-EM structures of HCV E2 glycoprotein bound to neutralizing and non-neutralizing antibodies determined using bivalent Fabs as fiducial markers

 

Fab CBH7

PDB

8TFE

Data collection and processing

 Wavelength (Å)

0.98

 Resolution range (Å)

46.14–1.62 (1.65–1.62)

 Space group

C121

 Unit cell parameters a, b, c (Å)

79.9, 101.9, 109.9

 α, β, γ

90.0, 100.2, 90.0

 Total (unique reflections)

689,842 (102,019)

 Completeness (%)

98.4 (98.5)

 Rmergea,b

0.09 (0.54)

 Ι/σ (Ι)a

27.75 (2.2)

 CC1/2c

0.99 (0.98)

 Multiplicitya

6.4 (5.6)

Refinement

 Rworkd(%)

17.8

 Rfreee(%)

21.4

RMSD from ideality

 

 Bond lengths (Å)

0.008

 Bond angles (°)

1.02

 Wilson B factor (Å2)

19.4

 Average B factor (Å2)

25.0

Ramachandran plot statistics

 

 Favored (%)

98

 Allowed (%)

2

 Outliers (%)

0

  1. aNumbers in parentheses refer to the highest resolution shell.
  2. bRmerge = Σ|Ij−<I>|/ΣIj, where Ij is the intensity of an individual reflection and <I> is the average intensity of that reflection.
  3. cCC1/2 is the Pearson correlation coefficient calculated between two random half data sets.
  4. dRwork = Σ||Fo|−|Fc||/Σ|Fo|.
  5. eRfree is as Rwork, but calculated with 5% of randomly chosen reflections omitted from refinement.
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