7RFO
SeMet Tailspike protein 4 (TSP4) phage CBA120, residues 1-335, obtained in the presence of LiSO4
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-04-15 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.97934 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 67.900, 67.900, 607.200 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 3.020 |
| R-factor | 0.2281 |
| Rwork | 0.225 |
| R-free | 0.29560 |
| Structure solution method | SAD |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.843 |
| Data reduction software | TRUNCATE |
| Data scaling software | Aimless |
| Phasing software | AutoSol |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.010 | 3.200 |
| High resolution limit [Å] | 3.020 | 3.020 |
| Rmerge | 0.228 | |
| Number of reflections | 28173 | 3193 |
| <I/σ(I)> | 20.4 | |
| Completeness [%] | 94.4 | |
| Redundancy | 66.9 | |
| CC(1/2) | 0.999 | 0.256 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7.5 | 295 | 1.6 M lithium sulfate, 0.1 M sodium chloride, 0.1 M HEPES, pH 7.5 |
