4CNR
Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture
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 | 2012-12-20 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 45.294, 141.114, 77.188 |
| Unit cell angles | 90.00, 90.07, 90.00 |
Refinement procedure
| Resolution | 45.290 - 2.290 |
| R-factor | 0.20177 |
| Rwork | 0.200 |
| R-free | 0.23594 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ml2 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.371 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.000 | 2.320 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.140 | 0.410 |
| Number of reflections | 48015 | |
| <I/σ(I)> | 12.9 | 4.1 |
| Completeness [%] | 97.9 | 95.7 |
| Redundancy | 7.5 | 7.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 5.5 | 281 | 10 MG/ML PROTEIN WITH 30% PEG 1500 AT 8C, pH 5.5 |
