Table 2 X-ray data collection and refinement statistics of CCR5–MIP-1α complex structure.
From: Structural basis for chemokine recognition and receptor activation of chemokine receptor CCR5
CCR5–MIP-1α | |
Data collectiona | |
Space group | C21 |
Cell dimensions | |
a, b, c (Å) | 49.1, 204.4, 69.0 |
α, β, γ (°) | 90.0, 105.5, 90.0 |
Resolution (Å) | 50.0–2.60 (2.64–2.60)b |
Rmerge (%) | 11.2 (94.2) |
I / σ(I) | 31.7 (1.3) |
CC1/2 (%) | 98.5 (80.8) |
Completeness (%) | 94.9 (75.6) |
Redundancy | 6.7 (5.7) |
Refinement | |
Resolution (Å) | 50.0–2.60 |
No. reflections | 17,242 (888) |
Rwork / Rfree (%) | 22.8/27.1 |
No. atoms | |
Protein | 3,375 |
Zn | 1 |
Average B-factors (Å2) | |
CCR5 | 111.1 |
MIP-1α | 119.8 |
Rubredoxin | 153.2 |
Zn | 225.4 |
R.m.s. deviations | |
Bond lengths (Å) | 0.011 |
Bond angles (°) | 1.604 |
Ramachandran plot | |
Favored (%) | 95.67 |
Allowed (%) | 4.33 |
Disallowed (%) | 0.00 |
