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. 2024 Feb 19;80(Pt 3):181–193. doi: 10.1107/S205979832400113X

Table 1. Crystallographic data-collection and refinement statistics.

Values in parentheses are for the outer shell.

  Mtr Re Mtr Ms
Data collection
 X-ray source ID23-2, ESRF ID30B, ESRF
 Detector PILATUS3 2M EIGER2 X 9M
 Temperature (K) 100 100
 Wavelength (Å) 0.87311 0.91840
 Space group P31 C2221
a, b, c (Å) 92.9, 92.9, 100.2 51.9, 209.6, 241.9
 α, β, γ (°) 90, 90, 120 90, 90, 90
 Rotation Standard Standard
 Rotation range per image (°) 0.1 0.2
 Total rotation range (°) 360 180
 Exposure time per image (s) 0.025 0.02
 Flux (photons s−1) 8.8 × 1010 1.1 × 1012
 Transmission (%) 6.2 10
 Beam size (µm) 4 × 4 10 × 10
 Crystal size (µm) 100 × 50 × 50 200 × 30 × 30
 Average diffraction-weighted dose (MGy) 9.7 27.0
 Mosaicity (°) 0.09 0.17
 Resolution range (Å) 46.5–2.90 (3.08–2.90) 49.4–4.70 (5.25–4.70)
 Total No. of reflections 219051 44357
 No. of unique reflections 21492 7284
R merge (%) 20.9 (172.4) 63.5 (118.3)
R p.i.m. (%) 6.9 (56.1) 27.8 (51.4)
 Completeness (%) 100 (100) 99.9 (99.9)
 Multiplicity 10.2 (10.3) 6.1 (6.3)
 〈I/σ(I)〉 10.1 (1.7) 3.0 (1.6)
 CC1/2 0.997 (0.593) 0.942 (0.847)
Refinement  
R work/R free (%) 17.7/22.3 29.3/33.8
 Mean overall B factor (Å2) 79.0 113.0
 Wilson B factor (Å2) 69.0 25.8
 Asymmetric unit content Homodimer Homodimer
 Protein residues in sequence 458 461
 Total modeled residues in asymmetric unit
  Protein residues by chain A, 458; B, 458 A, 461; B, 461
  Ligands by chain A, 1 FAD; B, 1 FAD
 Matthews coefficient (Å3 Da−1) 2.5 3.3
 Solvent content (%) 51.1 62.9
 Ramachandran plot    
  Favored (%) 95.7 81.4
  Allowed (%) 4.9 14.4
  Outliers (%) 4.2
 R.m.s.d., bond lengths (Å) 0.003 0.003
 R.m.s.d., bond angles (°) 0.752 0.826
 Estimated coordinate error (Å)
  Based on Luzzati plot 0.51 1.24
  Based on difference between F obs and F calc 0.55 1.23
  Based on diffraction-data precision index 0.38 1.57
 PDB code 8qcj 8qck