7R6S
Crystal Structure of the Putative Bacteriophage Protein from Stenotrophomonas maltophilia
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-01-29 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 0.97848 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 52.436, 90.670, 72.067 |
| Unit cell angles | 90.00, 103.99, 90.00 |
Refinement procedure
| Resolution | 28.710 - 1.900 |
| R-factor | 0.1905 |
| Rwork | 0.188 |
| R-free | 0.23080 |
| Structure solution method | SAD |
| RMSD bond length | 0.004 |
| RMSD bond angle | 1.269 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.082 | 0.928 |
| Rmeas | 0.090 | 1.022 |
| Rpim | 0.036 | 0.423 |
| Number of reflections | 51491 | 2592 |
| <I/σ(I)> | 20.1 | 2 |
| Completeness [%] | 98.9 | 99.6 |
| Redundancy | 5.9 | 5.6 |
| CC(1/2) | 0.999 | 0.705 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.6 | 292 | Protein: 8.4mg/ml, 0.15M Sodium chloride, 0.01M Tris pH 8.3; Screen: PEGs II (F6), 0.2M Ammonium sulfate, 0.1M tri-Sodium citrate pH 5.6, 25% (w/v) PEG 4000. |
