Table 1.
Data collection, MAD phasing, and refinement statistics.
| Native | Se-Met (Hsp104MMM) | |||
|---|---|---|---|---|
| Data Collection Statistics | ||||
| Space group | P 6522 | P 6522 | ||
| Unit Cell | a = 179.1 Å, b = 179.1 Å, c = 69.7 Å | a = 179.5 Å, b = 179.5 Å, c = 69.1 Å | ||
| α = 90°, β = 90°, γ = 120° | α = 90°, β = 90°, γ = 120° | |||
| Source | NSLS-X25 | NSLS-X25 | ||
| Wavelength (Å) | λ = 1.10 | λ1 = 0.9789 | λ2 = 0.9792 | λ3 = 1.0024 |
| Resolution (Å) | 41.53–2.82 | 44.8–3.5 | 44.8–3.5 | 44.8–3.8 |
| Completeness (%)a | 84.2 (12.7) | 99.8 (100) | 99.8 (99.5) | 99.9 (99.9) |
| Redundancy | 14.7 (1.7) | 6.9 (6.8) | 6.9 (6.5) | 6.7 (6.9) |
| Rsym a,b | 0.076 (0.386) | 0.086 (0.393) | 0.091 (0.497) | 0.088 (0.320) |
| I/σc | 17.6 | 12.9 | 11.1 | 10.7 |
| MAD Phasing Statistics | ||||
| Riso d | 0.222 | 0.044 | 0.053 | |
| RCullis e | 0.62 | 0.72 | ||
| Phasing Powerf | 2.38 | 2.07 | 1.16 | |
| Figure of Meritg | 0.63 (centric) | 0.60 (acentric) | ||
| Refinement Statistics | ||||
| Resolution (Å) | 41.53–2.82 | |||
| No. reflections | 14036 | |||
| Rcryst/Rfree | 0.210/0.279 | |||
| No. atoms | 2725 | |||
| Protein | 2721 | |||
| Water | 4 | |||
| B-factors | 94.1 | |||
| Protein | 94.1 | |||
| Water | 74.3 | |||
| rmsd bond (Å) | 0.002 | |||
| rmsd angle (°) | 0.399 | |||
| Ramachandran | ||||
| Favored (%) | 97.1 | |||
| Outliers (%) | 0.0 | |||
aValues for the highest resolution shell are given in parentheses. bRsym = Σhkl|I(hkl) − < I(hkl) > |/ΣhklI(hkl), where <I(hkl)> is the mean of the symmetry equivalent reflections of I(hkl). cBased on unmerged data. dRiso = Σ|FPH − FP|/ΣFp, where Fp is the peak (λ1), and FPH are the inflection (λ2), low energy remote (λ3) or native structure factor amplitudes. eRCullis = Σ||FPH ± FP| − FH calc|/Σ|FPH ± FP| for centric reflections only. fIsomorphous phasing power = Σ|FH|/Σ||FPH obs| − |FPH calc||; anomalous phasing power = Σ|F″H|/Σ||ADobs| − |ADcalc||. gFigure of Merit = weighted mean of the cosine of the deviation from αbest.