Table 2 X-ray data collection and refinement statistics.

From: In vitro evolution of an influenza broadly neutralizing antibody is modulated by hemagglutinin receptor specificity

Data collection

 

 Beamline

SSRL 12-2

 Wavelength (Å)

0.9795

 Space group

P43

 Unit cell parameters (Å)

a=b=88.3, c=255.0

 Resolution (Å)

50-1.97 (2.04-1.97)*

 Unique reflections

136,341 (13,627)*

 Redundancy

6.3 (6.2)*

 Completeness (%)

99.5 (99.5)*

 <I/σI>

15.4 (2.0)*

 Rsym†

0.16 (0.82)*

 Rpim†

0.07 (0.35)*

 CC1/2‡

0.99 (0.72)*

 Za§

2

Refinement statistics

 

 Resolution (Å)

50–1.97

 Reflections (work)

130,202

 Reflections (test)

6,751

 Rcryst(%)‖/Rfree(%)¶

18.1/20.8

 No. of atoms

 

Protein

 

 HA1

3,987

 Fab

6,846

Water

1,113

Ion

1

Glycan

56

Other#

90

 Average B-value (Å2)

 

Protein

 

 HA1

37.2

 Fab

30.5

Water

40.0

Ion

46.3

Glycan

74.4

Other#

77.2

 Wilson B-value (Å2)

22.7

R.m.s.d. from ideal geometry

 

 Bond length (Å)

0.013

 Bond angle (°)

1.60

Ramachandran statistics (%) **

 

 Favored

96.7

 Outliers

0.2

  1. r.m.s.d., root mean squared deviation.
  2. *Numbers in parentheses refer to the highest resolution shell.
  3. †Rsym=ΣhklΣi|Ihkl,i−<Ihkl>|/ΣhklΣiIhkl,i and Rpim=Σhkl(1/(n−1))1/2 Σi|Ihkl,i−<Ihkl>|/ΣhklΣiIhkl,i, where Ihkl,i is the scaled intensity of the ith measurement of reflection h, k, l, <Ihkl> is the average intensity for that reflection, and n is the redundancy.
  4. ‡CC1/2=Pearson correlation coefficient between two random half datasets.
  5. §Za is the number of HA1-Fab complexes per crystallographic asymmetric unit.
  6. ‖Rcryst=Σhkl|Fo−Fc|/Σhkl|Fo| × 100, where Fo and Fc are the observed and calculated structure factors, respectively.
  7. ¶Rfree was calculated as for Rcryst, but on a test set comprising 5% of the data excluded from refinement.
  8. #Other includes non-water solvent and cryoprotectant.
  9. **Calculated with MolProbity63.
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