4XAY
Cycles of destabilization and repair underlie evolutionary transitions in enzymes
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
Synchrotron site | Australian Synchrotron |
Beamline | MX1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-04-18 |
Detector | ADSC QUANTUM 210r |
Wavelength(s) | 0.9537 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 85.763, 85.923, 88.680 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.410 - 1.840 |
R-factor | 0.178 |
Rwork | 0.176 |
R-free | 0.21920 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4gy0 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.114 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | MOLREP |
Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 38.410 |
High resolution limit [Å] | 1.840 |
Rmerge | 0.107 |
Number of reflections | 57480 |
<I/σ(I)> | 16.17 |
Completeness [%] | 100.0 |
Redundancy | 7.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 277.15 | 100 mM Na Cacodylate, 30% methane-2,4-pentanediol |