Table 2. X-ray crystallographic data collection and refinement statistics.
| PDBID | 3KHW | 3KC6 | 3L56 |
| Protein | PB2, 538–741 | PB2, 538–741 | PB2, 538–759 |
| Strain | A/Mexico/INDRE4487/2009(H1N1) | A/Vietnam/1203/2004(H5N1) | A/Vietnam/1203/2004(H5N1) |
| Data Collection | |||
| space group | P212121 | P212121 | P21 |
| A | 53.86 | 33.08 | 41.04 |
| B | 68.19 | 65.69 | 57.00 |
| C | 107.35 | 96.85 | 83.08 |
| A | 90 | 90 | 90 |
| B | 90 | 90 | 102.4 |
| Γ | 90 | 90 | 90 |
| # molecules/asymmetric unit | 2 | 1 | 2 |
| Wavelength [Å] | 1.54178 | 1.54178 | 1.54178 |
| Resolution [Å](1) | 50.0–2.08 | 50.0–2.08 | 50–2.30 |
| (2.12–2.08) | (2.12–2.08) | (2.34–2.30) | |
| Redundancy | 6.8 (4.6) | 5.7 (4.4) | 3.5 (2.2) |
| Unique | 24405 (1121) | 13176 (621) | 16536 (678) |
| Completeness [%] | 99.5 (93.4) | 99.1 (96.6) | 98.1 (82.0) |
| Rmerge [%](2) | 7.4 (20.9) | 7.6 (27.7) | 2.9 (4.6) |
| I/σI(3) | 29.3 (5.6) | 25.5 (5.3) | 21.0 (18.5) |
| Mosaicity | 0.6 | 0.4 | 0.8 |
| Refinement Statistics | |||
| No. of reflections | 23670 (1626) | 12197 (861) | 16526 (940) |
| No. of non-hydrogen atoms | 3362 | 1607 | 3270 |
| Resolution range [Å] | 50–2.10 | 50.0–2.10 | 50–2.30 |
| (2.15–2.10) | (2.15–2.10) | (2.36–2.30) | |
| Rcryst (4) | 19.7 (18.5) | 19.9 (21.6) | 18.0 (19.8) |
| Rfree (5) | 23.8 (25.1) | 24.6 (34.3) | 23.7 (27.3) |
| FreeR, # of reflections | 5%, 1218 (88) | 5%, 631 (49) | 5%, 840 (53) |
| average Bfactor [Å2] | 7.8 | 9.8 | 12.9 |
| Model Geometry | |||
| Bond length deviation [Å] | 0.012 | 0.011 | 0.014 |
| Bond angle deviation [°] | 1.316 | 1.208 | 1.377 |
(1)
Numbers in parenthesis represent highest resolution shell of data.
(2)
R merge = (|ΣI hkl−<I>|/(ΣI hkl), where the average intensity <I> is taken over all symmetry equivalent measurements and I hkl is the measured intensity for any given reflection.
(3)
I/σI is the mean reflection intensity divided by the estimated error.
(4)
R cryst = ∥F o|−|F c∥/|F o|, where F o and F c are the observed and calculated structure factor amplitudes, respectively.
(5)
R free is equivalent to R cryst but calculated for 5% of the reflections chosen at random and omitted from the refinement process.