5NBV
Crystal structure of native alpha-1-antitrypsin with seven stabilising mutations
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I02 |
| Synchrotron site | Diamond |
| Beamline | I02 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-02-25 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 0.97630 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 113.700, 39.260, 90.560 |
| Unit cell angles | 90.00, 104.08, 90.00 |
Refinement procedure
| Resolution | 52.850 - 1.730 |
| R-factor | 0.21865 |
| Rwork | 0.216 |
| R-free | 0.25931 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5nbu |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.581 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0155) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 52.850 |
| High resolution limit [Å] | 1.730 |
| Number of reflections | 40844 |
| <I/σ(I)> | 7.4 |
| Completeness [%] | 99.8 |
| Redundancy | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | PEG 4000, carboxylic acid mixture |
