3M24
Crystal structure of TagBFP 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 | P 21 21 21 |
Unit cell lengths | 82.953, 105.943, 137.155 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.940 - 2.200 |
R-factor | 0.19558 |
Rwork | 0.193 |
R-free | 0.23803 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.293 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 1.950 |
Rmerge | 0.068 |
Number of reflections | 65147 |
<I/σ(I)> | 12 |
Completeness [%] | 89.1 |
Redundancy | 6.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 2.0 M ammonium sulfate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |