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 |