4CQH
Structure of Infrared Fluorescent Protein IFP2.0
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-09-17 |
Detector | MARRESEARCH |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 95.692, 52.912, 66.316 |
Unit cell angles | 90.00, 91.37, 90.00 |
Refinement procedure
Resolution | 27.330 - 1.140 |
R-factor | 0.13825 |
Rwork | 0.137 |
R-free | 0.15996 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2o9c |
RMSD bond length | 0.014 |
RMSD bond angle | 1.963 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.300 | 1.160 |
High resolution limit [Å] | 1.140 | 1.140 |
Rmerge | 0.060 | 0.640 |
Number of reflections | 114179 | |
<I/σ(I)> | 13.4 | 2.1 |
Completeness [%] | 99.8 | 99.7 |
Redundancy | 4 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4.6 | 30% PEG 400, 100 MM SODIUM ACETATE PH 4.6 |