3FO8
Crystal structure of the bacteriophage T4 tail sheath protein, protease resistant fragment gp18PR
Experimental procedure
| Experimental method | MAD |
| 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 | 2007-10-10 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97942, 0.97956, 0.97818 |
| Spacegroup name | F 4 3 2 |
| Unit cell lengths | 203.665, 203.665, 203.665 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 36.000 - 1.800 |
| R-factor | 0.191 |
| Rwork | 0.190 |
| R-free | 0.21900 |
| Structure solution method | MAD |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.013 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHELX (C/D/E) |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 36.000 | 1.840 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.064 | 0.794 |
| Number of reflections | 61873 | |
| <I/σ(I)> | 26.802 | 2 |
| Completeness [%] | 88.1 | 95.5 |
| Redundancy | 5.5 | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 1.2M Sodium acetate, 1M Imidazole pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
