8R13
Alpha-1-antitrypsin (Met374Phe) in the native conformation
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID30B |
| Synchrotron site | ESRF |
| Beamline | ID30B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-04-21 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.9763 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 114.982, 38.657, 89.244 |
| Unit cell angles | 90.00, 104.18, 90.00 |
Refinement procedure
| Resolution | 55.740 - 1.950 |
| R-factor | 0.2105 |
| Rwork | 0.209 |
| R-free | 0.23550 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.484 |
| Data reduction software | XDS (20180126) |
| Data scaling software | Aimless (0.6.2) |
| Phasing software | PHASER (2.3.0) |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 86.530 | 2.000 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.045 | 0.326 |
| Rmeas | 0.055 | 0.396 |
| Rpim | 0.031 | 0.223 |
| Total number of observations | 84082 | |
| Number of reflections | 27080 | 1855 |
| <I/σ(I)> | 13.7 | |
| Completeness [%] | 96.5 | |
| Redundancy | 3.1 | 3 |
| CC(1/2) | 0.998 | 0.971 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 293 | 22.5% PEG 1500, 0.1M MIB (malonate-imidazole-borate) pH 5.25 |
