Table 1.
Crystallographic Data
|
Native |
Se |
|||
|---|---|---|---|---|
| Space group | P41212 | P41212 | ||
| Cell dimensions (Å) | a=b=47.967, c=165.927 | a=b=47.802, c=164.116 | ||
| Inflection | Peak | Remote | ||
| Wavelength (Å) | 1.0076 | 0.97924 | 0.97900 | 0.93925 |
| Resolution (Å) (last shell) | 20.−2.1 (2.17–2.10) | 20.–2.2 (2.28–2.20) | 20.–2.2 (2.28–2.20) | 20.–2.2 (2.28–2.20) |
| Rmerge (%) (last shell) | 4.6 (17.0) | 7.9 (29.0) | 9.7 (31.3) | 8.8 (31.3) |
| <I/σI> (last shell) | 17.1 (10.5) | 9.1 (4.0) | 8.1 (3.6) | 8.1 (3.6) |
| Completeness (%) (last shell) | 97.8 (92.9) | 93.4 (78.3) | 93.6 (83.1) | 91.1 (76.3) |
| Unique reflections | 11,903 | 9709 | 9774 | 9510 |
| Redundancy | 9.7 | 10.4 | 10.0 | 10.6 |
| Phasing FOM (20.–3.0 Å) | 0.67 | |||
| Phasing power (20.–3.0 Å) | 1.1 | |||
| Number of residues | 185 | |||
| Number of Protein atoms | 1442 | |||
| Number of metal atoms | 3 | |||
| Number of bound waters | 112 | |||
| Rworking (last shell) | 0.238 (0.255) | |||
| Rfree (last shell) | 0.287 (0.277) | |||
| Average B factor for protein atoms (Å2) | 21.8 | |||
| Average B factor for metal atoms (Å2) | 43.1 | |||
| Average B factor for bound waters (Å2) | 27.3 | |||
| rms deviation from ideality | ||||
| bonds | 0.006 | |||
| angles | 1.205 | |||