4G9G
Crystal structures of N-acyl homoserine lactonase AidH E219G mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL44XU |
Synchrotron site | SPring-8 |
Beamline | BL44XU |
Temperature [K] | 180 |
Detector technology | CCD |
Collection date | 2011-07-22 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.378, 129.567, 44.728 |
Unit cell angles | 90.00, 111.02, 90.00 |
Refinement procedure
Resolution | 19.869 - 1.350 |
R-factor | 0.143 |
Rwork | 0.141 |
R-free | 0.17750 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4g5x |
RMSD bond length | 0.006 |
RMSD bond angle | 1.046 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX ((phenix.refine: 1.6.4_486)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.400 |
High resolution limit [Å] | 1.350 | 1.350 |
Number of reflections | 96822 | |
Completeness [%] | 51.4 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.3 | 293 | 35% PEG8000, 0.2M LiAc, 0.1M NaAc, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 293K |