5AGH
Crystal structure of the LeuRS editing domain of Candida albicans Mutant K510A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-03-04 |
Detector | MARMOSAIC 225 mm CCD |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 89.349, 41.104, 67.264 |
Unit cell angles | 90.00, 106.71, 90.00 |
Refinement procedure
Resolution | 64.420 - 1.810 |
R-factor | 0.16776 |
Rwork | 0.165 |
R-free | 0.21844 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2wfg |
RMSD bond length | 0.011 |
RMSD bond angle | 1.441 |
Data reduction software | DENZO |
Data scaling software | DENZO |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 64.000 | 1.850 |
High resolution limit [Å] | 1.810 | 1.810 |
Rmerge | 0.070 | 0.500 |
Number of reflections | 18976 | |
<I/σ(I)> | 20.8 | 2.6 |
Completeness [%] | 90.5 | 49 |
Redundancy | 4.9 | 4.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4 | 0.2 M AMMONIUM ACETATE, 0.1 M SODIUM ACETATE TRIHYDRATE PH 4.0, 24% PEG3350 |