Table 1 Crystallographic data collection and refinement statistics

From: Rationally designed carbohydrate-occluded epitopes elicit HIV-1 Env-specific antibodies

  C2S5 C4S3
Data collection   
Space group P3121 P212121
Cell dimensions   
 a, b, c (Å) 46.88, 46.88, 140.42 26.07, 57.61, 62.94
 α, β, γ (˚) 90, 90, 120 90, 90, 90
Resolution (Å) 50.00–2.00 (2.03–2.00)a 50.00–1.20 (1.22–1.20)
R merge 0.064 (0.886) 0.056 (0.130)
I / σI 13.6 (3.7) 18.9 (6.9)
Completeness (%) 99.67 98.40
Redundancy 18.0 (16.5) 14.1 (13.9)
No. of unique reflections 12904 30098
Refinement statistics   
Resolution (Å) 39.00–2.00 42.49–1.20
No. of reflections 12849 28610
Rwork/Rfree (%) 23.65/26.87 14.30/15.30
No. of atoms   
 Protein atoms 2344 771
 Ligand/ion 0 1 (SO42−)
 Water 17 67
Average B-factor (Å2)   
 Protein 70.43 7.54
 Ligand/ion NA 7.69
 Water 48.78 14.10
RMS deviation from ideality   
 Bond lengths (Å) 0.004 0.006
 Bond angles (°) 0.513 1.198
Ramachandran statisticsb   
 Favored regions (%) 99.28 89.20
 Allowed regions (%) 0.72 10.80
 Outliers (%) 0 0
  1. aHighest resolution shell statistics are shown in parentheses
  2. bAs defined by MolProbity