1RJQ
The crystal structure of the D-aminoacylase mutant D366A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSRRC BEAMLINE BL17B2 |
Synchrotron site | NSRRC |
Beamline | BL17B2 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2003-04-04 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.00 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 60.019, 76.927, 135.586 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 32.400 - 1.800 |
Rwork | 0.180 |
R-free | 0.20200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1m7j |
RMSD bond length | 0.005 |
RMSD bond angle | 1.410 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.060 | 0.220 |
Number of reflections | 53130 | |
<I/σ(I)> | 14.6 | 4.2 |
Completeness [%] | 89.7 | 87.3 |
Redundancy | 4 | 2.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 295 | PEG4000, ammonium acetate, sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 295K |