6HNU
Crystal structure of the aminotransferase Aro8 from C. Albicans with ligands
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BESSY BEAMLINE 14.2 |
Synchrotron site | BESSY |
Beamline | 14.2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-01-27 |
Detector | DECTRIS PILATUS 2M |
Wavelength(s) | 0.8943 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 69.785, 102.090, 146.883 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.330 - 1.800 |
R-factor | 0.17587 |
Rwork | 0.174 |
R-free | 0.21871 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6hnb |
RMSD bond length | 0.010 |
RMSD bond angle | 1.586 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0232) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.910 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.097 | |
Number of reflections | 97014 | 15338 |
<I/σ(I)> | 11.29 | 1.9 |
Completeness [%] | 99.6 | 98.6 |
Redundancy | 4.1 | 4.1 |
CC(1/2) | 0.997 | 0.687 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.2 M MgCl2, 0.1 M Bis-Tris pH 5.5, 25% PEG 3350 |