Table 1.
Summary of crystallographic data and refinement statistics
ASU, asymmetric unit; r.m.s., root mean square; CC1/2, Pearson's correlation coefficient.
| ApoCheR1 | MapZ–c-di-GMP–CheR1 | |
|---|---|---|
| Data collection | ||
| Space group | I41 | P212121 |
| Protein Data Bank code | 5Y4S | 5Y4R |
| Wavelength (Å) | 0.9779 | 0.9537 |
| Cell dimensions | ||
| a, b, c (Å) | 279.13, 279.13, 138.58 | 88.44, 98.82, 110.66 |
| α, β, γ (°) | 90, 90, 90 | 90, 90, 90 |
| Molecules/ASU | 10 | 2 |
| Resolution (Å)a | 50–3.41 (3.61–3.41) | 50–2.30 (2.44–2.30) |
| CC1/2 | 99.8 (53.1) | 99.8 (56.8) |
| I/σ(I) | 13.82 (1.42) | 12.64 (1.43) |
| Completeness (%)a | 99.9 (99.8) | 99.8 (99.0) |
| Redundancya | 14.5 (14.7) | 6.75 (6.91) |
| Refinement | ||
| Resolution (Å) | 49.42–3.41 | 48.29–2.30 |
| No. reflections | 143,720 | 83,410 |
| Rwork (Rfree) (%) | 25.7 (29.5) | 19.4 (23.9) |
| No. atoms | ||
| Protein | 20,244 | 6,230 |
| Ligand/ion | c-di-GMP, 184; SO4, 60 | |
| Water | 163 | |
| B-factors (Å2) | ||
| Protein | 246.3 | 59.4 |
| Ligand/ion | 60.7 | |
| Water | 50.9 | |
| r.m.s. deviations | ||
| Bond lengths (Å) | 0.004 | 0.011 |
| Bond angles (°) | 1.19 | 1.44 |
| Ramachandran plot | ||
| Favored (outlier) (%) | 90.0 (0.56) | 95.0 (0.26) |
a Values for the highest-resolution shell are in parentheses.