TABLE 2.
Data collection, phasing, and refinement statistics
| FrbF·acetyl-CoA | SeMet-labeled FrbF | |
|---|---|---|
| Data collection | ||
| Space group | P2 | P2 |
| Cell dimensions | a = 128.8, b = 35.7, c = 136.1 Å; β = 117.6° | a = 129.3, b = 36.5, c = 136.8 Å; β = 117.7° |
| Resolution (Å)a | 50–2.0 (2.11–2.0) | 50–3.0 (3.11–3.0) |
| Total reflections | 397,116 | 134,515 |
| Unique reflectionsa | 74,767 | 22,839 |
| Rsym (%) | 10.7 (47.5) | 11.4 (30.0) |
| I/σ(I) | 11.9 (2.4) | 15.5 (3.9) |
| Completeness (%) | 98.8 (96.0) | 97.5 (84.3) |
| Redundancy | 5.3 (5.2) | 5.9 (5.0) |
| Wilson B-value | 24.3 | 24.6 |
| FOM/FOM DMb | 0.32/0.79 | |
| Refinement | ||
| Resolution (Å) | 45.0–2.0 | |
| No. of reflections | 74,765 | |
| Rwork/Rfreec | 19.5/24.6 | |
| No. of atoms | ||
| Protein | 8139 | |
| Acetyl-CoA | 204 | |
| Water | 511 | |
| B-Factors | ||
| Protein | 35.4 | |
| Acetyl-CoA | 38.2 | |
| Water | 41.5 | |
| r.m.s.d.d | ||
| Bond lengths (Å) | 0.010 | |
| Bond angles | 1.11° | |
a Highest resolution shell is shown in parentheses.
b Figure of merit (defined as ∫φP(φ)eiφdφ, where P(φ) is the experimental phase probability distribution) is before (FOM) and after (FOM DM) density modification.
c Rwork = Σ(|Fobs| − k|Fcalc|)/Σ|Fobs|, and Rfree is the R-value for a test set of reflections consisting of a random 5% of the diffraction data not used in the refinement.
d r.m.s.d., root mean square deviation.