Table 1 Data processing and refinement statistics for GII.4 P-domain–NORO-320 Fab complex.

From: Broadly cross-reactive human antibodies that inhibit genogroup I and II noroviruses

Data collection

Beamline

ALS Beamline 5.0.1

Wavelength, Å

0.97741

Space group

P21 21 2

Cell dimensions, Å

119.25, 186.27, 73.44

α,β,γ,°

90, 90, 90

Resolution, Å

50–2.25 (2.29–2.25)a

Total reflections

1716311

Unique reflections

78053 (3854)a

Redundancy

6.5 (6.2)a

Completeness (%)

99.82

<I/sigma>

15.6875 (2.375)a

Rmeas b

0.129 (0.846)a

Rpimb

0.050 (0.340)a

Refinement statistics

Resolution, Å

50–2.25 (2.29–2.25)a

Reflections (work)

73965

Reflections (test)

3926

Rwork c /Rfree d (%)

18.08/22.55

No. of atoms

Protein

 

P-domain dimer

4798

Noro-320 Fab

6674

Water

1059

Average B Value (Å2)

P-domain dimer

34.2505

NORO-320 Fab

31.67

Water

36.085

RMSD from ideal geometry

Bond length (Å)

0.003

Bond angle (°)

0.614

Ramachandran statistics e

Favored

98.38%

Outliers

0.20%

  1. a Numbers in parentheses refer to the highest resolution shell.
  2. b Rmeas = Σhkl {N(hkl)/[N(hkl)-1]}1/2 X Σi | Ii(hkl)-{I(hkl)} |/ Σhkl ΣiIi(hkl) and Rpim = Σhkl (1/(n-1))1/2 Σi | Ihkl,i - | /Σhkl Σi Ihkl,i, where Ihkl,i is the scaled intensity of the ith measurement of reflection h, k, l, is the average intensity for that reflection, and n is the redundancy.
  3. c Rwork = Σhkl | FoFc | / Σhkl | Fo | × 100, where Fo and Fc are the observed and calculated structure factors, respectively.
  4. d Rfree was calculated as for Rwork, but on a test set comprising 5% of the data excluded from refinement.
  5. e Calculated with MolProbity48.