4EP0
Structure of the bacteriophage C1 tail knob protein, gp12
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 | 2011-10-21 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.03320 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 316.868, 211.380, 178.605 |
| Unit cell angles | 90.00, 116.53, 90.00 |
Refinement procedure
| Resolution | 49.726 - 4.000 |
| R-factor | 0.1969 |
| Rwork | 0.195 |
| R-free | 0.23320 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4eo2 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.392 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 8.600 | 4.070 |
| High resolution limit [Å] | 4.000 | 7.520 | 4.000 |
| Rmerge | 0.251 | 0.538 | |
| Number of reflections | 88253 | ||
| <I/σ(I)> | 8 | 3.5 | |
| Completeness [%] | 99.9 | 100 | 100 |
| Redundancy | 3.8 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 9.5 | 293 | 35% PEG400, 0.1 M CHES, pH 9.5, EVAPORATION, temperature 293K |
