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. 2020 Aug 25;32(11):3469–3484. doi: 10.1105/tpc.20.00067

Table 1. Data Collection and Refinement Statistics.

Parameter DNA-bound HD1CCT/GHD8/OsNF-YC2 GHD8/OsNF-YC2
Space group P 31 2 1 P 61
Cell dimensions
a, b, c (Å) 136.08, 136.08, 62.96 89.27, 89.27, 81.34
α, β, γ (°) 90, 90, 120 90, 90, 120
Wavelength (Å) 0.97914 0.97946
Resolution (Å) 45 ∼2.55 (2.66∼2.55) 45∼2.00 (2.05∼2.00)
Rmerge (%) 9.0 (80.0) 8.2 (58.0)
Rpim (%) 2.9 (26.7) 2.6 (18.1)
I/σ 14.8 (2.4) 21.2(5.3)
Completeness (%) 99.5 (99.2) 99.7 (98.0)
Number of measured reflections 217, 423 (24,970) 270, 613 (19,817)
Number of unique reflections 22, 041 (2,658) 25, 020 (1,825)
Redundancy 9.9 (9.4) 10.8 (10.9)
Wilson B factor (Å2) 45.5 22.3
Rwork/Rfree (%) 19.95/22.58 17.06/21.46
Number of atoms
Protein 1,708 2,737
Main chain 840 1,356
Side chain 868 1,381
Water molecules 16 168
Other entities (DNA) 1,025 0
All atoms 2,749 2,905
Average B value (Å2)
Protein 67.9 36.7
Main chain 64.6 31.9
Side chain 71.1 41.5
Water molecules 63.0 46.3
Other entities (DNA) 77.7 0
All atoms 71.5 37.3
Root mean square deviations
Bonds (Å) 0.010 0.007
Angle (°) 1.094 0.853
Ramachandran plot statistics (%)
Most favorable 96.1 98.5
Additionally allowed 3.9 1.5
Generously allowed 0 0

Values in parentheses are for the highest resolution shell. Rmerge = ΣhΣi|Ih,i-Ih|/ΣhΣiIh,i, where Ih is the mean intensity of the i observations of symmetry-related reflections of h. R = Σ|Fobs Fcalc|/ΣFobs, where Fcalc is the calculated protein structure factor from the atomic model (Rfree was calculated with 5% of the reflections selected).