5EHT
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 | 54.638, 55.735, 79.878 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 32.490 - 1.290 |
| R-factor | 0.12796 |
| Rwork | 0.126 |
| R-free | 0.16805 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5eh9 |
| RMSD bond length | 0.026 |
| RMSD bond angle | 2.203 |
| 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] | 32.490 |
| High resolution limit [Å] | 1.290 |
| Number of reflections | 61760 |
| <I/σ(I)> | 20.78 |
| Completeness [%] | 99.5 |
| Redundancy | 13.4 |
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 |
