Table 1. Data collection and refinement statistics.
| hRPTPσ Ig1-FN3 | cRPTPσ Ig1-2 +cTrkC LRRIg1cryst | cRPTPσ Ig1-3 +cTrkC LRRIg12Q | |
|---|---|---|---|
| Data collection | |||
| Space group | P6122 | P2 | P1 |
| Cell dimensions | |||
| a, b, c (Å) | 198.8, 198.8, 132.4 | 68.3, 122.2, 98.6 | 84.4, 93.1, 99.4 |
| α, β, γ (°) | 90.0, 90.0, 120.0 | 90.0, 109.8, 90.0 | 73.4, 89.5, 74.2 |
| Resolution (Å) | 99.40–3.15 (3.23–3.15)* | 63.96–2.50 (2.56–2.50) | 81.02–3.05 (3.13–3.05) |
| Rmerge | 7.8 (99.1) | 19.2 (142.4) | 6.9 (34.7) |
| Rpim† | 3.2 (41.0) | 5.7 (57.2) | 5.6 (60.3) |
| CC1/2‡ | 99.8 (63.9) | 99.5 (58.4) | 99.8 (67.2) |
| I/σI | 17.8 (2.1) | 10.7 (1.6) | 8.8 (1.5) |
| Completeness (%) | 95.6 (96.1) | 99.8 (99.3) | 96.3 (96.6) |
| Redundancy | 7.6 (7.5) | 11.6 (7.1) | 1.8 (1.8) |
| Refinement | |||
| Resolution (Å) | 99.40–3.15 (3.23–3.15) | 63.96–2.50 (2.56–2.50) | 81.02–3.05 (3.13–3.05) |
| No. reflections | 25,619 (1,858) | 52,652 (3,833) | 51,063 (3,823) |
| Rwork/Rfree | 23.4 (37.1)/26.5 (37.7) | 20.9 (32.2)/24.7 (36.2) | 22.6 (37.2)/24.0 (38.6) |
| No. of atoms | |||
| Protein | 4,380 | 8,536 | 10,630 |
| NAGs | 2 | 5 | 1 |
| SO42− ions | — | 2 | — |
| Water | — | 118 | — |
| B-factors | |||
| Protein | 122.2 | 57.2 | 116.4 |
| NAGs | 153.0 | 83.0 | 176.3 |
| SO42− ions | — | 90.9 | — |
| Water | — | 45.0 | — |
| R.m.s.d. | |||
| Bond lengths (Å) | 0.005 | 0.008 | 0.006 |
| Bond angles (°) | 1.008 | 1.243 | 1.045 |
RPTP, Receptor protein tyrosine phosphatase; r.m.s.d., root mean squared deviation.
*Values in parentheses are for highest-resolution shell. Each structure is based on a single crystal.
†Rpim (the precision-indicating merging R-value)=1/(N−1) × Rmerge, where N is the redundancy.
‡CC1/2 is the mean intensity correlation coefficient of half-data sets53.