5FB4
Crystal structure of the bacteriophage phi29 tail knob protein gp9 truncation variant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U |
Synchrotron site | SSRF |
Beamline | BL17U |
Temperature [K] | 160 |
Detector technology | CCD |
Collection date | 2014-10-03 |
Detector | RAYONIX MX-225 |
Wavelength(s) | 0.978 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 94.600, 135.161, 313.431 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.317 - 2.039 |
R-factor | 0.1547 |
Rwork | 0.153 |
R-free | 0.18320 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5fei |
RMSD bond length | 0.008 |
RMSD bond angle | 1.053 |
Data scaling software | HKL-2000 |
Phasing software | SHARP |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.320 | |
High resolution limit [Å] | 2.039 | |
Number of reflections | 126814 | |
<I/σ(I)> | 17.66 | 9.2 |
Completeness [%] | 99.3 | 95.11 |
Redundancy | 6.1 | 5.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293.15 | 0.94% v/v ethanol, 10% PEG-400, HEPES buffer pH 7.5, magnesium chloride |