TABLE 1.
Summary of the data collection phasing, and refinement statistics for selenomethionyl n1α_LNS#2
| Data seta | Resolutionb | Reflections (total/unique) | Completeness | Rmergec | I/σ | Phasing powerd | Rcullisd (iso/ano) |
|---|---|---|---|---|---|---|---|
| Å | % | ||||||
| FII | 2.1 (2.18–2.1) | 190,980/52,304 | 98.1 (96.6) | 8.9 (32.4) | 16.4 (2.7) | 2.13 | 0.77/0.76 |
| FI | 2.1 (2.18–2.1) | 191,448/52,276 | 98.2 (96.9) | 9.0 (29.1) | 18.0 (3.1) | 1.74 | 0.83/0.86 |
| LR | 2.1 (2.18–2.1) | 187,261/51,547 | 96.6 (85.9) | 7.2 (26.5) | 16.6 (2.9) | ||
| Figure of merit 10 to 3 Å: 0.619 for 16 selenium sites | |||||||
| Model | Value | ||||||
|
| |||||||
| Resolution (Å) | 20.0–2.1 (all reflections |F|/σ ≥ 0.0) | ||||||
| Protein atoms | 5,553 (727 residues) | ||||||
| Solvent atoms | 443 | ||||||
| Ligands | 4 Ca2+ ions, 4 glycerol molecules | ||||||
| Unique reflections | 51,492 | ||||||
| Working set/test set | 48,915/2,577 | ||||||
| Rwork (%) | 18.4 | ||||||
| Rfree (%) | 23.3 | ||||||
| r.m.s.d. bond lengths (Å) | 0.011 | ||||||
| r.m.s.d. bond angles (degrees) | 1.391 | ||||||
| r.m.s.d. between NCS-related molecules (Å) | 0.435 Å (181 Cα atoms) average over 4 molecules | ||||||
| Average B of main/side-chain atoms (Å2)e | 35.6 Å2 for 2,908 main-chain atoms/36.7 Å2 for 2,645 side-chain atoms | ||||||
| Average B of solvent atoms (Å2)e | 41.5 Å2 for 444 solvent molecules | ||||||
| Average B of Ca2+ ions (Å2)e | 26.0 Å2 for 4 ions | ||||||
a
FII (peak, 0.97895 Å), FI (inflection, 0.97934 Å), and LR (low energy remote 0.98011 Å).
b
Outer shell statistics are in parentheses.
c
Rmerge = Σ(|(I−〈Imean〉)|)/Σ(I).
d
Phasing power = 〈Fh〉/εand Rcullis = ε/δ iso, where ε is the lack of closure. The phasing power and Rcullis are calculated for data between 10 and 3 Å.
e
After TLS refinement by REFMAC.