5NBU
Crystal structure of native alpha-1-antitrypsin with seven stabilising mutations
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I04 |
Synchrotron site | Diamond |
Beamline | I04 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2013-02-26 |
Detector | DECTRIS PILATUS 6M-F |
Wavelength(s) | 0.97630 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 114.100, 39.340, 89.410 |
Unit cell angles | 90.00, 103.70, 90.00 |
Refinement procedure
Resolution | 55.430 - 1.670 |
R-factor | 0.18037 |
Rwork | 0.178 |
R-free | 0.22840 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ne4 |
RMSD bond length | 0.020 |
RMSD bond angle | 1.905 |
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] | 55.430 |
High resolution limit [Å] | 1.670 |
Number of reflections | 44986 |
<I/σ(I)> | 7.5 |
Completeness [%] | 99.5 |
Redundancy | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | PEG 4000, carboxylic acid mixture |