Table 1. Data collection and refinement statistics of KLC1-TPR and KLC2-TPR.
| KLC1-TPR | KLC2-TPR | |
| Data collection | ||
| Space group | P3121 | P212121 |
| Cell dimensions | ||
| a, b, c (Å) | 74.7, 74.7, 156.2 | 70.4, 99.9, 103.1 |
| Wavelength | 0.92015 | 0.9790 |
| Resolution (Å) | 2.80 (2.90–2.80) | 2.75 (2.85–2.75) |
| R sym a(%) | 6.8 (58.4) | 14.4 (41.2) |
| I/σI | 43.8 (1.8) | 16.5 (2.2) |
| Completeness (%) | 97.2 (78.7) | 94.3 (82.2) |
| Redundancy | 8.6 (3.8) | 13.3 (5.8) |
| Refinement | ||
| Resolution (Å) | 29.88–2.80 | 30.0–2.75 |
| No. reflections | 12597 | 19197 |
| R work/R free b (%) | 20.0/27.3 | 23.6/27.1 |
| No. atoms | ||
| Protein | 2149 | 4089 |
| Ligand/ion | ||
| Water | 2 | |
| B-factors (Å2) | ||
| Protein | 94.5 | 77.1 |
| R.m.s deviations | ||
| Bond lengths (Å) | 0.01 | 0.01 |
| Bond angles (°) | 1.1 | 0.85 |
| PDB code | 3NF1 | 3CEQ |
a
Rsym = Σ|I-<I>|/ΣI.
b
Rwork = Σ||F0|-|Fc||/Σ|F0|, where F0 and Fc are the observed and calculated structure factors, respectively. Rfree was calculated as Rwork using 4.6% and 5.1% of the data selected for KLC1-TPR and KLC2-TPR respectively.