4O8G
Structure of Infrared Fluorescent Protein 1.4
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-08-21 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.6 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 96.162, 53.228, 66.796 |
Unit cell angles | 90.00, 90.60, 90.00 |
Refinement procedure
Resolution | 24.040 - 1.652 |
R-factor | 0.18606 |
Rwork | 0.185 |
R-free | 0.21073 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3s7n |
RMSD bond length | 0.009 |
RMSD bond angle | 1.508 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.700 |
High resolution limit [Å] | 1.620 | 1.650 |
Number of reflections | 38000 | |
<I/σ(I)> | 29.7 | 8.84 |
Completeness [%] | 93.7 | 99.9 |
Redundancy | 7.1 | 6.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 295 | Mother liquor 6% PEG 4000, 10% glycerol, 0.07 M sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 295K |