3M22
Crystal structure of TagRFP fluorescent protein
Experimental procedure
Experimental method | SAD |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-04-17 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.08 |
Spacegroup name | I 41 |
Unit cell lengths | 130.989, 130.989, 105.966 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 34.800 - 2.200 |
R-factor | 0.161 |
Rwork | 0.160 |
R-free | 0.17900 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.012 |
RMSD bond angle | 1.681 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASES |
Refinement software | REFMAC |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 1.950 |
Rmerge | 0.149 |
Number of reflections | 50406 |
<I/σ(I)> | 3.8 |
Completeness [%] | 85.5 |
Redundancy | 4.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.8 | 298 | 30% PEG 4000, 0.1 M Tris-HCl, pH 8.5, 0.2 M MgCl2, 0.1 M TCEP, VAPOR DIFFUSION, SITTING DROP, temperature 298K |