Table 1 X-ray diffraction data collection and structure refinement statistics.
| Â | 6LSE: S6A/S6B (C3) | 6LSF: S6RA/S6RB (C3) | 6LSG: S6M (C0) | 6LSH: S6M (C2) |
|---|---|---|---|---|
Data collectiona | ||||
Space group | P212121 | P212121 | P212121 | P212121 |
Cell dimensions | ||||
a, b, c (Ã…) | 62.6, 77.0, 156.7 | 61.4, 76.4, 155.0 | 63.6, 77.2, 154.2 | 62.9, 77.4, 155.8 |
α, β, γ (◦) | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 |
Resolution (Å)b | 50.00–2.25 (2.33–2.25) | 50.00–2.15 (2.23–2.15) | 50.00–2.12 (2.20–2.12) | 50.00-2.23 (2.31-2.23) |
No. unique reflections | 32,014 | 36,176 | 42,624 | 35,885 |
Rmerge | 0.082 (0.52) | 0.061 (0.34) | 0.029 (0.16) | 0.036 (0.42) |
Rmeas | 0.092 (0.60) | 0.076 (0.47) | 0.034 (0.23) | 0.049 (0.58) |
CC1/2 | 0.992 (0.77) | 0.999 (0.88) | 0.999 (0.98) | 1.002 (0.84) |
I/σI | 13.7 (2.1) | 16.8 (2.6) | 44.6 (6.9) | 31.9 (2.5) |
Completeness (%) | 87.2 (75.2) | 89.5 (66.8) | 96.9 (69.4) | 95.2 (79.1) |
Redundancy | 4.4 (3.6) | 4.7 (3.7) | 6.2 (4.5) | 5.5 (3.9) |
Structure refinement | ||||
Resolution (Ã…) | 2.25 | 2.15 | 2.12 | 2.23 |
Rwork/Rfreec (%) | 19.9/24.0 | 21.5/25.1 | 19.0/21.7 | 20.8/24.5 |
No. atoms | ||||
Protein/RNA | 3616/340 | 3629/405 | 3,638/386 | 3,617/405 |
Ligand/Ion/Water | 19/1/170 | 5/1/92 | 5/1/228 | 5/1/103 |
B-factors (Ã…2) | ||||
Protein/RNA | 45.7/49.3 | 53.1/65.0 | 43.4/54.7 | 54.4/74.0 |
Ligand/Ion/Water | 56.2/32.5/44.8 | 48.4/44.6/49.6 | 37.9/36.3/44.4 | 48.1/45.7/50.9 |
RMSD | ||||
Bond lengths (Ã…) | 0.007 | 0.008 | 0.007 | 0.008 |
Bond angles (â—¦) | 0.851 | 0.9 | 0.833 | 0.851 |
