Table 1. Data collection and refinement statistics.
ScS1-ADP | ScS1-SO4 | |
---|---|---|
Data collection | ||
Resolution range, Å | 50.0-3.10 | 38.79-2.75 |
Unique reflections | 21,662 | 31,951 |
Multiplicity | 4.5 | 4.0 |
Average I/σ | 27.2 | 20.5 |
Rsym, % (all data/outer shell) | 10.2/39.3 | 4.8/38.5 |
Completeness, % (all data/outer shell) | 89.4/78.8 | 88.0/81.8 |
Refinement | ||
σ cutoff | 0.0 | 2.0 |
Completeness in range, % | 84.6 | 76.3 |
R factor, % | 23.3 | 24.2 |
Rfree, % (5% partition) | 26.9 | 28.6 |
Mean B-factor | 80.5 | 57.1 |
rms deviations* | ||
Bond lengths, Å | 0.006 | 0.011 |
Bond angles,° | 1.6 | 1.4 |
No. of protein atoms | 8,578 | 8,661 |
No. of water atoms | 1 | 95 |
No. of prosthetic atoms | 33 | 8 |
Cross-validated coordinate error, ņ | 0.47 | 0.5 |
The cell parameters of the two structures are as follows: ScS1-ADP, P21: a = 84.1 Å, b = 50.9 Å, c = 161.6 Å, α = 90.0°, β = 98.4°, and γ = 90.0°; ScS1-SO4, P21: a = 83.6 Å, b = 51.1 Å, c = 162.3 Å, α = 90.0°, β = 98.0°, and γ = 90.0°. Eighty-two percent of the ScS1-SO4 residues and 83% of the ScS1-ADP residues in the final models are in the most favored regions of the Ramachandran plot, with the rest in additionally allowed regions.
See ref. 46.