Table 1. Data collection and refinement statistics (molecular replacement).
D2-06-N2 5D1Q | D4-30-N2 5D1X | D4-10-N1 5D1Z | |
---|---|---|---|
Data collection | |||
Space group | P 42 21 2 | P 41 | P 2 21 21 |
Cell dimensions | |||
a, b, c (Å) | 121.3, 121.3, 193.2 | 111.3, 111.3, 105.2 | 115.2, 147.1, 164.9 |
α, β, γ (°) | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 |
Resolution (Å) | 47.33–3.22 | 49.18–3.21 | 24.96–3.17 |
Rsym or Rmerge | 9.6 (53.6) | 11.1 (46.3) | 15.6 (56.8) |
I/σI | 20.4 (3.4) | 10.8 (1.97) | 7.6 (1.95) |
Completeness (%) | 98.8 | 98.9 | 97.9 |
Redundancy | 6.6 (6.6) | 3.3 (3.1) | 3.5 (3.4) |
Refinement | |||
Resolution (Å) | 3.22 | 3.21 | 3.17 |
No. reflections | 22,680 | 19,661 | 45,212 |
Rwork/Rfree | 21.7/28.1 | 27.1/30.9 | 23.7/28.6 |
No. atoms | |||
Protein | 7,583 | 6,684 | 15,717 |
Ligand/ion | — | — | — |
Water | — | — | — |
B-factors | |||
Protein | 93.787 | 87.022 | 49.474 |
Ligand/ion | — | — | — |
Water | — | — | — |
R.m.s. deviations | |||
Bond lengths (Å) | 0.012 | 0.009 | 0.012 |
Bond angles (°) | 1.697 | 1.465 | 1.539 |
One crystal used for each structure. *Values in parentheses are for highest-resolution shell.