Data collection, phasing, and refinement statistics
. | Human Notch1 NRR . |
---|---|
Data collection | |
Space group | C2 |
Cell dimensions | |
a, b, c, Å | 169.9, 91.8, 59.8 |
α, β, γ, ° | 90, 109, 90 |
Resolution, Å | 50.0-2.0 (2.07-2.0)* |
Rsym | 4.6 (20.2) |
I / σI | 23.3 (3.2) |
Completeness (%) | 93.1 (60.7) |
Redundancy | 3.5 (2.4) |
Refinement | |
Resolution, Å | 30.0-2.0 |
No. reflections | 52 098 |
Rwork/Rfree | 21.3/25.2 |
No. atoms | |
Protein | 3580 |
Ligand/ion | 8 |
Water | 282 |
Glycerol | 7 |
Overall B-factors | 43.6 |
R.m.s deviations | |
Bond lengths, Å | 0.015 |
Bond angles, ° | 1.47 |
. | Human Notch1 NRR . |
---|---|
Data collection | |
Space group | C2 |
Cell dimensions | |
a, b, c, Å | 169.9, 91.8, 59.8 |
α, β, γ, ° | 90, 109, 90 |
Resolution, Å | 50.0-2.0 (2.07-2.0)* |
Rsym | 4.6 (20.2) |
I / σI | 23.3 (3.2) |
Completeness (%) | 93.1 (60.7) |
Redundancy | 3.5 (2.4) |
Refinement | |
Resolution, Å | 30.0-2.0 |
No. reflections | 52 098 |
Rwork/Rfree | 21.3/25.2 |
No. atoms | |
Protein | 3580 |
Ligand/ion | 8 |
Water | 282 |
Glycerol | 7 |
Overall B-factors | 43.6 |
R.m.s deviations | |
Bond lengths, Å | 0.015 |
Bond angles, ° | 1.47 |
Highest resolution shell is shown in parentheses.