6OFO
Crystal structure of split green fluorescent protein (GFP); s10 circular permutant (194-195)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL12-2 |
Synchrotron site | SSRL |
Beamline | BL12-2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-07-04 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.9795 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 50.749, 51.070, 97.298 |
Unit cell angles | 90.00, 103.67, 90.00 |
Refinement procedure
Resolution | 39.043 - 2.603 |
R-factor | 0.2042 |
Rwork | 0.203 |
R-free | 0.23550 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2b3p |
RMSD bond length | 0.005 |
RMSD bond angle | 0.741 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHENIX |
Refinement software | PHENIX ((1.13rc2_2986: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.043 | 2.690 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmeas | 0.192 | 1.790 |
Number of reflections | 14682 | 1109 |
<I/σ(I)> | 6.43 | 0.8 |
Completeness [%] | 92.3 | 71.6 |
Redundancy | 3.7 | 3.6 |
CC(1/2) | 0.990 | 0.553 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277 | 0.1 M MES, pH 6.5, 20% MPD |