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 |