5SWC
The structure of the beta-carbonic anhydrase CcaA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08ID-1 |
| Synchrotron site | CLSI |
| Beamline | 08ID-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-06-10 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 0.97888 |
| Spacegroup name | I 4 |
| Unit cell lengths | 202.950, 202.950, 70.510 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.816 - 1.450 |
| R-factor | 0.1309 |
| Rwork | 0.131 |
| R-free | 0.14650 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ekj |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.418 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.816 | 1.500 |
| High resolution limit [Å] | 1.340 | 1.450 |
| Rmerge | 0.613 | |
| Number of reflections | 317226 | |
| <I/σ(I)> | 15.01 | 2.55 |
| Completeness [%] | 99.0 | 99.5 |
| Redundancy | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 293 | 7.1 mg/ml protein, 2.0 M Na formate, 0.1 M Na acetate |
