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[Preprint]. 2024 Jun 1:2024.05.25.595513. Originally published 2024 May 25. [Version 2] doi: 10.1101/2024.05.25.595513

Table 2. X-ray diffraction data processing and crystal structure refinement.

The values in parentheses correspond to the highest-resolution shell.

Nanobody 5E 7E 8C 8D 10E
Data processing
Space group P312 P1 P21 P1 P212121
Unit cell parameters 110.8, 110.8, 83.3 Å; 90, 90, 120 ° 37.2, 79.0, 117.6 Å; 77.7, 87.7, 84.3 ° 39.86, 54.17, 80.4 Å; 90, 96.36, 90 ° 42.30, 46.54, 91.99 Å; 95.65, 100.11, 90.08 ° 101.7, 118.3, 122.5 Å; 90, 90, 90 °
Resolution range (Å) 50–2.75 (3.15–2.75) 50–2.50 (2.56–2.50) 50–1.73 (1.77–1.73) 50–1.50 (1.59–1.50) 50–2.55 (2.62–2.55)
⟨I/σI⟩ 10.3 (1.6) 5.5 (0.6) 11.8 (1.0) 6.9 (0.5) 11.6 (0.5)
Completeness (%) Spherical 70.0 (18.0) [ellipsoidal 99.6(66.7)] 91.7 (91.3) 99.1 (98.7) 89.7 (89.4) 99.8 (99.8)
Redundancy 5.6 (6.3) 3.8 (3.8) 5.6 (6.3) 2.7 (2.7) 7.5 (7.4)
Rmeas (%) 14.2 (136.3) 20.5 (291.4) 8.0 (225.6) 9.1 (236.8) 11.2 (349.6)
CC½ (%) 99.6 (58.0) 99.2 (33.5) 99.8 (35.9) 99.7 (22.4) 99.9 (33.5)
Structure refinement
Rcryst/Rfree (%) 28.9/32.3 25.4/29.9 19.0/21.5 17.9/22.9 28.0/30.3
RMSD bond lengths (Å)/angles (°) 0.002/0.6 0.004/0.7 0.011/1.1 0.011/1.0 0.005/0.7
Ramachandran favoured/outliers (%) 89.5/2.1 95.1/0.8 97.2/0.6 98.1/0.0 94.4/0.9
MolProbity score/percentile 2.86/68th 2.22/89th 1.74/77th 1.24/96th 2.48/80th
Protein chains in asymmetric unit 2 8 2 4 8
PDB entry 9ERT 9ERU 9ERW 9ETL 9ETJ