Table 1. Crystallographic data collection and structure refinement statistics.
Data set | Kv4.2 T1 |
Wavelength, Å | 1.54 |
Cell a, b, c, Å | a = 60.0, b = 60.0, c = 61.6 |
Space group | P4212 |
Resolution, Å | 2.1 |
Completeness, % | 99.5 |
Rmerge,* % | 5.5 |
Rcryst,† % | 23.04 |
Rfree,‡ % | 27.7 |
No. reflections | 163,537 |
No. unique reflections | 7,071 |
Reflections in test set, % | 10.8 |
No. protein atoms | 885 |
No. water molecules | 57 |
Avg. B factor, Å2 | 30 |
Rmerge = Σ|li — 〈l〉|/Σ li.
Rcryst = Σ|Fo — Fc|/Σ|Fo|.
Rfree = Σ|Fo — Fc|/Σ|Fo| for a 10.8% subset of diffraction data.