5AJG
Structure of Infrared Fluorescent Protein IFP1.4 AT 1.11 Angstrom resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2013-11-21 |
Detector | DECTRIS PILATUS 6M |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 95.361, 53.028, 66.219 |
Unit cell angles | 90.00, 90.90, 90.00 |
Refinement procedure
Resolution | 38.430 - 1.110 |
R-factor | 0.14693 |
Rwork | 0.146 |
R-free | 0.16806 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4cqh |
RMSD bond length | 0.014 |
RMSD bond angle | 1.944 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 38.400 | 1.130 |
High resolution limit [Å] | 1.110 | 1.110 |
Number of reflections | 121711 | |
<I/σ(I)> | 17.6 | 2 |
Completeness [%] | 98.5 | 92.1 |
Redundancy | 4.3 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5 | 26% PEG 400, 0.1 M SODIUM ACETATE PH 5.0 |