Table 5.
Data collection and refinement statistics for crystals. Data collection statistics computed in HKL200020, refinement statistics computed in CCP428 and CNS21, as described under “Experimental Procedures”.
| Data Collection | SurA(ΔP2)/C-peptide | P1/C-peptide | P1/N-peptide |
|---|---|---|---|
| Spacegroup | P3221 | P21 | C222 |
| Unit cell parameters (Å) | a=148.33, c=188.68 | a=56.46, b=50.63, c=74.06, β=111.54° | a=51.89, b=98.82,c=41.05 |
| Wavelength (Å) | 1.000 | 1.000 | 1.000 |
| Resolution range (last shell) (Å) | 50.0-3.39 (3.52-3.39) | 50.0-1.30 (1.35-1.30) | 50.0-1.29 (1.34-1.29) |
| Unique reflections | 33486 (3326) | 93257 (8714) | 26586 (2504) |
| Completeness (%) | 99.1 (99.8) | 90.2 (96.2) | 93.8 (98.4) |
| Redundancy | 4.2 (3.5) | 2.2 (2.5) | 4.5 (3.5) |
| Rsyma
|
0.074 (0.422) | 0.045 (0.250) | 0.034 (0.126) |
|
Refinement
|
|||
| Resolution range (last shell) (Å) | 41.8-3.39 (3.48-3.39) | 50.0-1.30 (1.38-1.30) | 50.0-1.30 (1.38-1.30) |
| Rcrystb | 0.286 (0.479) | 0.208 (0.256) | 0.226 (0.250) |
| Rfree | 0.298 (0.456) | 0.227 (0.281) | 0.243 (0.293) |
| Number of reflections (working set) | 31581 (2237) | 81232 (11419) | 23302 (3351) |
| Number of reflections (test set) | 1690 (143) | 9046 (1357) | 2552 (419) |
| Number of protein atoms | 4532 | 3324 | 839 |
| Number of water molecules | 0 | 398 | 132 |
| Average B value, protein (Å2) | 177.0 | AB dimerc: 15.9
CD dimer: 18.0 |
17.3 |
| Average B value, peptide (Å2) | 182.2 | Ec: 16.4
F: 18.8 |
22.3 |
| Rmsd bond length (Å) | 0.010 | 0.006 | 0.009 |
| Rmsd angles (°) | 1.26 | 1.48 | 1.58 |
| Ramachandran analysis | |||
| Residues in most favored regions | 80.5% | 95.0% | 93.3% |
| Residues in additional allowed regions | 17.8% | 5.0% | 6.7% |
| Residues in generously allowed regions | 1.3% | none | none |
| Residues in disallowed regions | 0.4% | none | none |
a
Rsym = Σ|Ihkl − <Ihkl>|/Σ<Ihkl> where Ihkl = single value of measured intensity of hkl reflection, and <Ihkl> = mean of all measured value intensity of hkl reflection.
b
Rcryst = Σ|Fobs−Fcalc|/ΣFobs where Fobs = observed structure factor amplitude and Fcalc = structure factor calculated from model. Rfree is computed in the same manner as Rcryst, using the test set of reflections. Numbers in parentheses are for highest resolution shell.
c
Letters refer to chain IDs in PDB file 2PV2.