5EGK
The structural and biochemical characterization of acyl-coa hydrolase mutant Asp43Ala from Staphylococcus aureus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-03-31 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9537 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 49.710, 129.000, 83.560 |
Unit cell angles | 90.00, 104.10, 90.00 |
Refinement procedure
Resolution | 29.960 - 2.400 |
R-factor | 0.2081 |
Rwork | 0.206 |
R-free | 0.23840 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4ncp |
RMSD bond length | 0.008 |
RMSD bond angle | 1.224 |
Data reduction software | iMOSFLM |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX ((1.10pre_2104: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.960 | 2.486 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.075 | 0.470 |
Number of reflections | 39444 | |
<I/σ(I)> | 7.63 | 2.1 |
Completeness [%] | 98.9 | 98.62 |
Redundancy | 2 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 296 | 1.6 M Ammonium Phosphate monobasic, 0.1 Sodium citrate tribasic pH 4.5 |