5IO1
CRYSTAL STRUCTURE OF RECOMBINANT HUMAN Z ALPHA-1-ANTITRYPSIN
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX14.2 |
| Synchrotron site | SRS |
| Beamline | PX14.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-11-29 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.988 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 74.138, 53.675, 110.144 |
| Unit cell angles | 90.00, 96.88, 90.00 |
Refinement procedure
| Resolution | 48.230 - 3.340 |
| R-factor | 0.2184 |
| Rwork | 0.215 |
| R-free | 0.27460 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1qlp |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.799 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 74.540 | 3.520 |
| High resolution limit [Å] | 3.340 | 3.340 |
| Rmerge | 0.125 | 0.811 |
| Number of reflections | 12404 | |
| <I/σ(I)> | 10.9 | 1.5 |
| Completeness [%] | 99.0 | 96.5 |
| Redundancy | 4.3 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 6.5 | 293 | 20-30% PEG8000, 0.2M NACL, 0.1M MES, PH 6.5, EVAPORATION, TEMPERATURE 298K |
