Table 2.1.
Selected crystallographic data.
| Data Collection | XlKu80-KBMAPLF (PDB: 6TYZ) |
XlKu80-KBMMRI (PDB:6TYU) |
XlKu80-KBMWRN (PDB:6TYV) |
|---|---|---|---|
| Space Group | P212121 | P212121 | P212121 |
| Unit Cell [a,b,c] | 43.8, 71.2, 79.5 | 44.6, 71.4, 79.2 | 44.6, 71.4, 79.2 |
| Wavelength [Å] | 1.54 | 1.54 | 1.54 |
| X-ray Source | Cu | Cu | Cu |
| Resolution [Å] (Highest shell) | 50–1.51 (1.54–1.51) | 50–1.47 (1.50–1.47) | 50–1.92 (1.95–1.92) |
| No. of Reflections [unique] | 234,283 (39,709) | 212,709(43,410) | 94,595 (18,919) |
| Completeness [%] | 99.8 (98.2) | 99.1 (88.3) | 99.5 (99.0) |
| Rsyma [%] | 4.6 (45.5) | 4.4 (47.2) | 6.4 (41.4) |
| I/σ | 50.0 (2.5) | 53.0 (2.3) | 34.3 (3.2) |
| Redundancy | 5.9 (3.3) | 4.9 (2.1) | 5.0 (3.2) |
| Refinement | |||
| Resolution [Å] (Highest shell) | 29.5–1.51 (1.55–1.51) | 37.8–1.47 (1.50–1.47) | 37.52–1.92(2.02–1.92) |
| Molecules per AU | 1 | 1 | 1 |
| No. of a.a.(XlKu80)/AU | 209 | 209 | 207 |
| No. of a.a.(Peptide)/AU | 12 | 11 | 13 |
| No. of waters/AU | 172 | 192 | 113 |
| Rworking b [%] | 17.8 | 20.2 | 19.0 |
| Rfree c [%] | 20.4 | 22.0 | 22.2 |
| Average B factor [Å2] | |||
| Protein | 28.9 | 30.0 | 45.3 |
| Peptide | 26.8 | 27.9 | 53.5 |
| Water | 37.3 | 40.8 | 46.3 |
| RMS deviations | |||
| Bonds [Å] | 0.007 | 0.008 | 0.008 |
| Angles [°] | 0.831 | 0.906 | 0.831 |
| Ramachandran [%] | |||
| Favored, Allowed, Outlier | 98.2, 1.8, 0 | 98.2, 1.8, 0 | 96.4, 3.4, 0 |
a
Rsym = ΣΣ|I- 〈I〉|/ ΣΣ|I|, where I is the observed intensity and <I> is the average intensity.
b
Rworking = Σ||Fo|-|Fc||/ Σ|Fo, where Fo and Fc are the observed and calculated structure factors, respectively.
c
Rfree = Σ||Fo|-|Fc||/ Σ|Fo| for 5 % of the data not used at any stage of the structural refinement.