TABLE 3.
Data collection and refinement statistics for the εGs crystal structure
| Statistic | In-house dataa | Synchrotron dataa | |
|---|---|---|---|
| Data collection | |||
| Space group | P 1 21 1 | P 1 21 1 | |
| Cell dimensions | |||
| a, b, c (Å) | 35.65, 82.78, 83.43 | 36.54, 83.21, 83.43 | |
| α, β, γ (°) | 90, 92.76, 90 | 90, 93.28, 90 | |
| Peak | Remote | ||
| Wavelength | 1.54179 | 0.97941 | 0.95369 |
| Resolution (Å) | 25.0–2.3 (2.42–2.3) | 41.65–2.31 (2.44–2.31) | 41.33–2.3 (2.42–2.3) |
| Observations | 158,061 (22,673) | 138,779 (22,137) | 139,240 (22,352) |
| No. of unique reflections | 21,590 (3,136) | 19,757 (3,096) | 19,727 (22,352) |
| Rmerg | 0.056 (0.237) | 0.097 (0.749) | 0.076 (0.489) |
| Rmeas | 0.060 (0.255) | 0.135 (0.856) | 0.098 (0.566) |
| Mean I/σ(I) | 18.4 (5.9) | 11.8 (2.9) | 14.2 (3.6) |
| Completeness (%) | 99.92 (100.00) | 90.1 (96.8) | 91.5 (97.5) |
| Multiplicity | 7.3 (7.2) | 7.0 (7.2) | 7.1 (7.2) |
| Anomalous completeness (%) | 90.3 (97.0) | 90.9 (97.0) | |
| Anomalous multiplicity (%) | 3.6 (3.6) | 3.6 (3.7) | |
| Wilson B-factors | 46.36 | 35 | 34.2 |
| Refinement | |||
| Resolution (Å) | 23.07–2.30 (2.38–2.30) | ||
| No. of reflections | 21,575 (2,185) | ||
| Rwork | 0.214 (0.267) | ||
| Rfree | 0.256 (0.314) | ||
| CC*b | 0.819 (0.648) | ||
| CCwork | 0.890 (0.903) | ||
| CCfree | 0.873 (0.791) | ||
| No. of atoms | 6,955 | ||
| Protein | 3,506 | ||
| Ligand/ion | |||
| Water | 37 | ||
| B-factors | |||
| Overall | 61.7 | ||
| Protein | 61.9 | ||
| Ligand/ion | |||
| Water | 42.1 | ||
| RMS deviations | |||
| Bond lengths (Å) | 0.004 | ||
| Bond angles (°) | 0.72 | ||
| Ramachandran favored (%) | 97 | ||
| Ramachandran outliers (%) | 0.53 | ||
a
Values for the highest-resolution shell are shown in parentheses.
b
CC*, true correlation coefficient, as defined by the phenix tool.