Table 1.
Crystallographic data and refinement statistics
| A. Crystal data | ||
| Crystal | CI101-229DM K192A | CI101-229DM |
| Space group | P6122 | P6122 |
| Cell dimensions (Å) | a = b=59.6, c = 148.5 | a=b=59.6, c=148.4 |
| Resolution (Å) | 30-1.8 | 30-2.5 |
| Observed reflections | 119,808 | 31,534 |
| Unique reflections | 15,045 | 5891 |
| Completeness (%) | 97.6 (83.2)a | 99.6 (99.1) |
| Redundancy | 7.9 (2.12) | 5.3 (5.6) |
| Rmerge (%)b | 6.6 (31.0) | 10.9 (33.6) |
| I/σ | 18.6 (3.2) | 10.7 (4.9) |
| B. Refinement statistics | ||
| Number protein atoms | 1,007 | 998 |
| Number water molecules | 120 | 80 |
| Number of reflections (working/free set) | 13,101/1944 | 5066/825 |
| R-factor (%)c | 25.2 (43.6) | 25.3 (31.1) |
| Free R-factor (%)c | 28.2 (46.9) | 32.1 (39.1) |
| Estimated coordinate error (Å)d | 0.32 | 0.49 |
| Mean B-factor (Å2) | 32.4 | 33.4 |
| RMS deviation from ideality: | ||
| Bonds (Å) | 0.005 | 0.006 |
| Angles (°) | 1.3 | 1.2 |
a
Numbers in parentheses refer to the highest resolution shell only
b
Rmerge=Σ|Ih − <I>h|/Σ Ih, where <I>h is average intensity over symmetry equivalents, and h is reflection index. I/σ is the mean of the intensity/sigma of the unique averaged reflections.
c
R-factor=Σ|Fobs − Fcalc|/ΣFobs. R free is calculated from 10% of the reflections that are omitted from the refinement.
d
The estimated coordinate error is the value from the cross-validated sigma plot.