TABLE 1.
Data collection and refinement statistics
| P2(7–289) | P2(15–275)* | |||
|---|---|---|---|---|
| Data collectiona | APS 23ID-D | APS 23ID-B | ||
| Space group | P212121 | F222 | ||
| Cell dimensions | ||||
| a, b, c | 43.7 Å, 89.5 Å, 125.6 Å | 83.6 Å, 86.1 Å, 162.8 Å | ||
| α, β, γ | 90°, 90°, 90° | 90°, 90°, 90° | ||
| Native | Peak | Inflection | Remote | |
|
|
||||
| Wavelength | 0.9793 Å | 0.9795 Å | 0.9796 | 0.9495 Å |
| Resolution limit | 3.25 Å | 1.8 Å | 1.8 Å | 1.9 Å |
| Rsymb | 0.16 (0.46) | 0.1 (0.5) | 0.074 (0.43) | 0.08 (0.456) |
| <I/σ> | 19.0 (4.5) | 37 (2.4) | 41.7 (2.6) | 32 (2.9) |
| Completeness (%) | 99.9 (99.0) | 98.5 (86.9) | 98.4 (86.8) | 99.3 (93.7) |
| Redundancy | 8.4 (7.7) | 8.2 (3.9) | 8.4 (4.8) | 8.6 (5.7) |
|
| ||||
| Refinement | ||||
| Resolution limits | 45 – 3.25 Å | 43.1 – 1.8 Å | ||
| No. of reflections | 8,229 | 27,047 | ||
| R factor (Rfree)c | 0.25 (0.32) | 0.21 (0.24) | ||
|
| ||||
| Model | ||||
| Protein | 2 × P2(7–289) aa 15–27, 39–66, 71–120, 132–197, 203–282d |
1 × P2(15–275)* aa 15–27, 38–119, 130–196, 202–258 1 sulfate ione, 130 water molecules |
||
| Total number atoms | 3,221 | 1,836 | ||
| R.M.S deviations | ||||
| bond lengths | 0.010 Å | 0.014 Å | ||
| bond angles | 1.262° | 1.510° | ||
a
Numbers in parentheses refer to last resolution shell
b
Rsym = Σ|Ih-<Ih>|/ΣIh, where <Ih> = average intensity over symmetry equivalent measurements
c
R factor = Σ|Fo-Fc|/ΣFo, where summation is over data used in the refinement; Rfree includes only 5% of the data excluded from the refinement
d
Numbers in Table are for chain A. For chain B: aa 16–26, 40–64, 73–119, 130–196, 204–269
e
Sulfate ion is at special position, modeled with half occupancy