Table 1 Data collection and refinement statistics (molecular replacement).
From: Structural basis of the dynamic human CEACAM1 monomer-dimer equilibrium
V39A (PDB code 6XNW) | I91A (PDB code 6XNT) | E99A (PDB code 6XNO) | N97A (PDB code 6XO1) | |
|---|---|---|---|---|
Data collection | ||||
Space group | P 3 | P 4212 | P 4212 | C 2221 |
Cell dimensions a, b, c (Å) α, β, γ (o) | 91.4, 91.4, 64.4, 90.0, 90.0, 120.0 | 102.1, 102.1, 61.0, 90.0, 90.0, 90.00 | 106.8, 106.8, 62.2, 90.0, 90.0, 90.00 | 55.9,56.8,124.5, 90.0, 90.0, 120.0 |
Resolution (Å) | 39.59–1.90 (1.94–1.90) | 72.21–3.1 (3.31–3.1) | 75.5–1.9(1.94–1.90 | 28.76–1.76 (1.8–1.76) |
Rmerge (%), | 18.8 (155.1) | 24.6(75.4) | 11.9 (140.3) | 8.6 (833) |
I/ σI | 7.8 (1.4) | 9.4 (3.8) | 14.3 (2.3) | 19.5 (2.0) |
Completeness (%) | 100 (100) | 100 (100) | 100 (100) | 96.1(73.2) |
Redundancy | 7.7 (7.6) | 11.7 (11.7) | 13.6 (13.3) | 11.9 (6.2) |
Refinement | ||||
Resolution (Å) | 39.59–1.90 (1.94–1.90) | 72.21–3.1 (3.31–3.1) | 75.5–1.9(1.94–1.90 | 28.76–1.76 (1.8–1.76) |
No. reflectionsa | 366913 (23237) | 73320 (12990) | 393727(24522) | 231087 (6712) |
Rwork/Rfree | 14.5 / 18.6 | 22.1 / 25.8 | 18.9 / 22.3 | 19.2/24.0 |
No. atoms | ||||
Protein | 3356 | 1676 | 1674 | 1676 |
Ligand/ion | 2 | 40 | 54 | 14 |
Water | 15 | 4 | 86 | 181 |
B-factors | ||||
Protein | 28.10 | 42.48 | 30.26 | 15.15 |
Ligand/ion | 21.17 | 63.02 | 55.84 | 34.20 |
Water | 26.28 | 33.46 | 38.15 | 23.60 |
R.m.s.deviations | ||||
Bond-lengths (Å) | 0.021 | 0.014 | 0.021 | 0.019 |
Bond-angles (°) | 2.27 | 1..85 | 2.15 | 1.91 |
