Table 1.
X-ray Diffraction Data and Refinement Statistics
| Diffraction Data | |||
|---|---|---|---|
| Crystal | IpgC10-155 | IpgC21-155 | |
| Beamline | APS 22 - BM | APS 22-ID | |
| Wavelength (Å) | 1.000 | 1.000 | |
| Space Group | P21 | P31 or P32 | |
| Cell Constants | a = 140.50 | a = 86.11 | |
| b = 71.47 | b = 86.11 | ||
| c = 171.01 | c = 476.27 | ||
| ß = 93.86° | |||
| Resolution (Å) | 50-3.30 | 50-3.40 | |
| Completeness (%) | 88.5 (49.6) | 89.3 (79.1) | |
| Total Reflections | 151,044 | 89,308 | |
| Unique Reflections | 45,608 | 48,191 | |
| Redundancy | 3.4 | 1.9 | |
| Rmerge(%)a | 14.9 (50.7) | 10.0 (33.2) | |
| I/σ | 7.3 (1.4) | 7.0 (1.8) | |
| Refinement | |||
| Rwork/Rfreeb | 25.9/29.6 | ||
| B factor (Å2) | 98.23 | ||
| RMSD | |||
| Bond Length (Å) | 0.011 | ||
| Bond Angle (°) | 1.29 | ||
| Dihedral Angle (°) | 19.67 | ||
| Ramachandran | |||
| Favored (%) | 91.50 | ||
| Allowed (%) | 5.80 | ||
| Protein atoms | 20,070 | ||
aRmerge = ΣhΣi|Ii(h)-<I(h)>|/ΣhΣiIi(h), where Ii(h) is the ith measurement of reflection h and <I(h)> is a weighted mean of all measurements of h.
bR = Σh|Fobs(h)-Fcalc(h)|/Σh|Fobs|. Rcryst and Rfree were calculated from the working and test reflection sets, respectively. The test set constituted 5% of the total reflections not used in refinement.