5A25
Rational engineering of a mesophilic carbonic anhydrase to an extreme halotolerant biocatalyst
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 | 2011-04-27 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 59.331, 79.440, 61.521 |
| Unit cell angles | 90.00, 106.98, 90.00 |
Refinement procedure
| Resolution | 58.840 - 1.900 |
| R-factor | 0.15532 |
| Rwork | 0.153 |
| R-free | 0.19689 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1v9e |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.766 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0107) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.900 | 1.980 |
| High resolution limit [Å] | 1.880 | 1.880 |
| Rmerge | 0.090 | 0.380 |
| Number of reflections | 41643 | |
| <I/σ(I)> | 19.5 | 4.4 |
| Completeness [%] | 93.8 | 68.3 |
| Redundancy | 7.4 | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.2 | 150 NL 20 MG/ML PROTEIN PLUS 150 NL RESERVOIR CONSISTING OF 50 MM TRIS PH 8.2, 2.3 M AMMONIUM SULFATE, 0.023 (W/V) N-OCTYL-B-D-GLUCOPYRANOSIDE |
