2QUG
Crystal structure of alpha-1-antitrypsin, crystal form A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-BM-C |
| Synchrotron site | APS |
| Beamline | 14-BM-C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-03-20 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 113.368, 39.391, 90.154 |
| Unit cell angles | 90.00, 104.61, 90.00 |
Refinement procedure
| Resolution | 87.370 - 2.000 |
| R-factor | 0.218 |
| Rwork | 0.215 |
| R-free | 0.27500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.381 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 87.370 | 2.110 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.139 | 0.708 |
| Total number of observations | 16785 | |
| Number of reflections | 24296 | |
| <I/σ(I)> | 8.1 | 2 |
| Completeness [%] | 91.9 | 90.8 |
| Redundancy | 4.8 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 295 | 29% PEG 3350, 400 mM NaF, vapor diffusion, hanging drop, temperature 295K |
