Table 1.
X-Ray Diffraction Data Collection and Refinement Statistics of sFlaF
| sFlaF native 1 | sFlaF native 2 | sFlaF + Pt | |
|---|---|---|---|
| Data Collection | |||
| Synchrotron beamline | ALS 12.3.1 | ALS 12.3.1 | ALS 12.3.1 |
| PDB code | 4ZBH | 4P94 | |
| Wavelength (Å) | 0.9677 | 1.0332 | 0.9677 |
| Space group | P43212 | I 2 3 | P43212 |
| Cell dimensions | |||
| a, b, c (Å) | 52.41, 52.41, 100.24 | 127.26, 127.26, 127.26 | 52.71, 52.71, 99.30 |
| α, β, γ (°) | 90.00, 90.00, 90.00 | 90.00, 90.00, 90.00 | 90.00, 90.00, 90.00 |
| Resolution (Å)a | 50.00–1.50 (1.55–1.50) |
44.99–1.65 (1.68–1.65) |
50.00–2.50 (2.59–2.50) |
| Observations | 127,605 | 770,110 | 71,034 |
| Unique observation | 22,839 | 41,166 | 5,275 |
| Rsyma,b | 0.051 (0.516) | 0.054 (0.591) | 0.080 (0.409) |
| Mean I/σIa | 62.6 (3.7) | 30.4 (4.0) | 51.2 (8.0) |
| Completeness (%)a | 98.4 (97.6) | 100 (100) | 100 (100) |
| Redundancy | 5.6 | 18.7 | 13.5 |
| Refinement | |||
| Rwork/Rfree (%)c | 15.8/19.6 | 17.3/20.0 | |
| Rmsd bond length (Å) | 0.005 | 0.007 | |
| Rmsd bond angles (°) | 1.052 | 1.062 | |
| Protein molecules in asymmetric unit | 1 | 2 | |
| Residues not in model | 35–45 | Chain A: 35–48 | |
| Average B-factor | |||
| Protein | 26.10 | 23.50 | |
| Solvent | 45.60 | 37.60 | |
| Ramachandran (%) | |||
| Most favored | 97.44 | 97 | |
| Additional allowed | 2.56 | 3 | |
| Generous allowed | 0 | 0 | |
| Disallowed | 0 | 0 | |
a
Values in parentheses are the statistics for the highest-resolution shell of data.
b
Rsym = S |Ihkl − <I>|/S<I>, where <I> is the average individual measurement of Ihkl.
c
Rwork = (S|Fobs − Fcalc|)/S|Fobs|, where Fobs and Fcalc are the observed and calculated structure factors, respectively. Rfree is calculated the same as Rwork but from the data (5%) that were excluded from the refinement.