Table 1 Data collection and refinement statistics.
From: Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family
KdHpuA | KdHpuA (cobalt SAD) | NgHpuA-C | KdHpuA:Hb complex | |
|---|---|---|---|---|
Data collection | ||||
Space group | P43212 | P43212 | H3 | P21 |
Cell dimensions | ||||
a, b, c (Å) | 102.5, 102.5, 77.2 | 103.4, 103.4, 77.0 | 61.9, 61.9, 92.2 | 54.8, 87.2, 124.3 |
α, β, γ (°) | 90.0, 90.0, 90.0 | 90, 90, 90 | 90, 90, 120 | 90, 98.1, 90 |
Resolution (Å) | 26.67–1.60 (1.69–1.60)* | 28.68–1.94 (2.05–1.94) | 34.97–1.95 (2.06–1.95) | 41.53–2.30 (2.42–2.30) |
Rmerge | 0.102 (0.853) | 0.140 (0.671) | 0.084 (0.54) | 0.175 (0.818) |
I/σI | 12.6 (2.8) | 14.9 (4.0) | 9.1 (2.3) | 8.6 (2.1) |
Completeness (%) | 100 (100) | 100 (100) | 99.8 (99.9) | 96.9 (97.8) |
Redundancy | 11.4 (11.4) | 18.8 (17.9) | 4.0 (3.9) | 6.5 (6.3) |
Refinement | ||||
Resolution (Å) | 72.46–1.6 | 46.4–1.95 | 123.1–2.3 | |
No. reflections | 51939 | 9078 | 47357 | |
Rwork/Rfree | 0.171 / 0.196 | 0.178 / 0.23 | 0.202 / 0.244 | |
No. atoms | ||||
Protein | 2278 | 916 | 8742 | |
Ligand/ion | 12 | 0 | 192 | |
Water | 328 | 58 | 374 | |
B-factors | ||||
Protein | 24.79 | 39.00 | 33.55 | |
Ligand/ion | 48.53 | 30.05 | ||
Water | 34.14 | 45.13 | 33.21 | |
Root mean squared deviations | ||||
Bond lengths (Å) | 0.014 | 0.011 | 0.013 | |
Bond angles (°) | 1.608 | 1.384 | 1.504 | |
