Table 1. Statistics for data collection, phasing, and model refinement.
| Data collection and phasinga | |
| Space group | P 21 21 21 |
| Cell dimensions | |
| a, b, c (Å), α, β, γ (°) | 34.32, 64.04, 113.66, 90, 90, 90 |
| Data set | Se λ1 (peak) |
| X-ray wavelength (Å) | 0.9794 |
| Resolution range (Å)b | 32.86–1.50 (1.53–1.50) |
| <I/σ(I)> | 12.1 (2.5) |
| Multiplicity | 12.2 (6.9) |
| Unique reflections | 40,943 (2,566) |
| Completeness (%) | 99.5 (95.9) |
| Rmerge (%)c | 0.5 (54.3) |
| Figure of meritd for SAD phasing: 0.44 | |
| Refinement | |
| Rwork e/Rfree f | 0.144/0.170 |
| No. of protein atoms | 1,666 |
| No. of water atoms | 332 |
| No. of Non-water atoms | 75 |
| Mean B value (Å2) | 18.9 |
| Ramachandran plot analysis (for Chain A) | |
| Most favored regions | 198 (96.6%) |
| Additional allowed regions | 7 (3.4%) |
| Disallowed regions | 0 (0%) |
| R.m.s. deviations from ideal geometry | |
| Bond lengths (Å) | 0.017 |
| Bond angles (°) | 1.91 |
a
Data collected at the Sector 23-ID-D of the Advanced Photon Source.
b
Numbers in parentheses indicate the highest resolution shell of 20.
c
Rmerge = Σh Σi |I(h)i–<I(h)>|/Σh Σi I(h)i, where I(h) is the observed intensity of reflection h, and <I(h)> is the average intensity obtained from multiple measurements.
d
Figure of merit = <|Σ P(α)eiα/Σ P(α)|>, where α is the phase angle and P(α) is the phase probability distribution.
e
Rwork = Σ | |Fo|–|Fc| |/Σ |Fo|, where |Fo| is the observed structure factor amplitude and |Fc| is the calculated structure factor amplitude.
f
Rfree = R-factor based on 5.0% of the data excluded from refinement.