Table I. X-ray diffraction data collection and refinement statistics.
| Motor protein | WT Kar3+N11 | Kar3 N650K | Kar3 R598A | Kar3 E631A |
|---|---|---|---|---|
| Space group | P21 | P21 | P21 | P43 |
| Cell dimensions | ||||
| a (Å) | 43.6 | 43.6 | 43.9 | 62.9 |
| b (Å) | 78.8 | 78.0 | 77.4 | – |
| c (Å) | 47.2 | 47.3 | 47.7 | 153.6 |
| β (°) | 105.0 | 105.1 | 105.9 | – |
| Data collection | ||||
| resolution (Å) | 20.0–1.5 | 20.0–1.7 | 20.0–1.3 | 20.0–2.5 |
| measured reflections | 793 427 | 309 408 | 929 216 | 265 649 |
| unique reflections | 47 889 | 31 822 | 70 750 | 20 874 |
| completeness (%, > –3σ)a | 97.3 (94.9) | 93.5 (89.5) | 94.0 (87.8) | 96.0 (66.9) |
| Rsym (%)b | 7.4 | 7.0 | 4.6 | 8.5 |
| average I/σ(I) | 16.2 | 17.5 | 41.7 | 18.8 |
| Refinement | ||||
| Rworkc | 0.213 | 0.217 | 0.218 | 0.230 |
| Rfree (%)c | 0.243 | 0.266 | 0.242 | 0.276 |
| number of reflections [F > 2σ (F)] | 41 892 | 27 632 | 67 836 | 18 420 |
| number of protein atoms | 2 393 | 2 444 | 2 470 | 4 746 |
| number of non-protein atoms | 317 | 237 | 424 | 191 |
| r.m.s.d.d bond length (Å) | 0.006 | 0.006 | 0.006 | 0.009 |
| r.m.s.d.d bond angles (°) | 1.20 | 1.19 | 1.22 | 1.42 |
| average B factors (Å2, main chain/side chain) | 19.6/22.3 | 22.3/24.6 | 15.2/17.8 | 42.3/44.8 |
aLast shell values are in parentheses. The last shell includes the resolution between 1.53 and 1.50 Å in Kar3+N11, 1.73 and 1.7 Å in Kar3 N650K, 1.32 and 1.3 Å in Kar3 R598A, and 2.59 and 2.5 Å in Kar3 E631A.
bRsym = Σhkl[Σi |Ihkl,i – <Ihkl>|]/Σhkl,i<Ihkl>, where Ihkl,i is the intensity of an individual measurement of the reflection with Miller indices h, k and l, and <Ihkl> is the mean intensity of that reflection.
cRwork = Σ||Fobs| – |Fcalc||/Σ|Fobs|, where |Fobs| and |Fcalc| are observed and calculated structure factor amplitudes, respectively. Rfree is equivalent to Rwork except that 10% of the total reflections were set aside to test the progress of refinement.
dR.m.s. deviation from ideal geometry.