3FCZ
Adaptive protein evolution grants organismal fitness by improving catalysis and flexibility
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1.7 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 69.670, 48.810, 77.190 |
Unit cell angles | 90.00, 109.86, 90.00 |
Refinement procedure
Resolution | 72.599 - 2.804 |
R-factor | 0.197 |
Rwork | 0.194 |
R-free | 0.25810 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2bc2 |
RMSD bond length | 0.005 |
RMSD bond angle | 0.777 |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 100.000 |
High resolution limit [Å] | 2.800 |
Rmerge | 0.103 |
Number of reflections | 8961 |
<I/σ(I)> | 11.2 |
Completeness [%] | 73.6 |
Redundancy | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 291 | 24% PEG 3350, 0.1M sodium tartrate, 1mM DTT, 1mM zinc acetate, 0.1M sodium cacodylate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |