2C9I
Structure of the fluorescent protein asFP499 from Anemonia sulcata
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ELETTRA BEAMLINE 5.2R |
Synchrotron site | ELETTRA |
Beamline | 5.2R |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 71.880, 135.126, 95.071 |
Unit cell angles | 90.00, 106.93, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.820 |
R-factor | 0.248 |
Rwork | 0.245 |
R-free | 0.29200 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 1.387 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.050 | 0.190 |
Number of reflections | 128068 | |
<I/σ(I)> | 17.5 | 2 |
Completeness [%] | 87.3 | 81.4 |
Redundancy | 5.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8.5 | 30 PERCENT PEG 4000, 0.1 M TRIS PH 8.5, 0.2 M MAGNESIUM CHLORIDE |