5EH9
Indirect contributions of mutations underlie optimization of new enzyme function
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-02-10 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.0332 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.511, 55.473, 79.358 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.470 - 1.290 |
R-factor | 0.11693 |
Rwork | 0.115 |
R-free | 0.15347 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3dhb |
RMSD bond length | 0.026 |
RMSD bond angle | 2.244 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | MOLREP |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 45.470 |
High resolution limit [Å] | 1.290 |
Number of reflections | 61128 |
<I/σ(I)> | 16.33 |
Completeness [%] | 99.8 |
Redundancy | 7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 291 | 25% (w/v) PEG 4 K, 20% (v/v) glycerol, 80 mM Tris-HCl, pH 8.5, 160 mM MgCl2 |