Table 2.
Crystallographic data collection and refinement statistics
| Crystal | Cu Bs-YcnIΔC | Apo Bs-YcnIΔC |
|---|---|---|
| Protein Data Bank accession code | 7MEK | 7ME6 |
| Data collection | ||
| Wavelength (Å)a | 1.377 | 0.979 |
| Space group | P6322 | P6322 |
| Cell dimensions | ||
| a, b, c (Å) | 90.2, 90.2, 209.1 | 90.4, 90.4, 208.4 |
| α, β, γ (°) | 90, 90, 120 | 90, 90, 120 |
| Resolution (Å) | 30–2.11 (2.16–2.11)b | 39.1–2.05 (2.11–2.05)b |
| Rmeas (%) | 13.8 (152.7)b | 13.8 (134.5)b |
| I/σI | 9.64 (2.64)b | 12.06 (1.77)b |
| Completeness (%) | 99.6 (98.0)b | 99.8 (97.4)b |
| Redundancy | 5.3 (5.3)b | 11.1 (8.1)b |
| Refinement | ||
| Resolution (Å) | 29.52–2.11 (2.14–2.11)b | 38.48–2.05 (2.10–2.05)b |
| No. of reflections | 54,321 | 32,328 |
| Rwork/Rfree (%) | 19.5/21.7 (30.8/30.9)b | 19.6/21.9 (26.3/29.3)b |
| Residue range built | A: 27–155, B: 27–153 | A: 27–155, B: 27–154 |
| No. of atoms | ||
| Protein | 2027 | 2040 |
| Ligand/ion | 2 Cu | 2 malonate |
| Water | 125 | 252 |
| Model quality | ||
| B-factors (Å2) | ||
| Overall | 47.05 | 48.16 |
| Protein | 46.84 | 47.72 |
| Ligand/ion | 54.78 | 71.61 |
| Water | 50.35 | 50.36 |
| RMSD, bond lengths (Å) | 0.002 | 0.007 |
| RMSD, bond angles (°) | 0.526 | 0.98 |
| Ramachandran favored/allowed/outliers (%) | 97.33/2.78/0 | 98.81/1.19/0 |
a
1 Å = 0.1 nm.
b
Values shown in parentheses are for the highest resolution shell.