3FOA
Crystal structure of the bacteriophage T4 tail sheath protein, deletion mutant gp18M
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-06-06 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97857 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 99.590, 116.290, 433.760 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.795 - 3.500 |
| R-factor | 0.2687 |
| Rwork | 0.267 |
| R-free | 0.29900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3fo8 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.985 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.630 |
| High resolution limit [Å] | 3.500 | 3.500 |
| Rmerge | 0.106 | 0.291 |
| Number of reflections | 32322 | |
| <I/σ(I)> | 11.905 | |
| Completeness [%] | 87.8 | 61.1 |
| Redundancy | 3.7 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | PEG 20000, MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
