2EFU
The crystal structure of D-amino acid amidase from Ochrobactrum anthropi SV3 complexed with L-phenylalanine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL38B1 |
Synchrotron site | SPring-8 |
Beamline | BL38B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-09-24 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 77.468, 123.274, 116.156 |
Unit cell angles | 90.00, 104.05, 90.00 |
Refinement procedure
Resolution | 47.670 - 2.300 |
R-factor | 0.17373 |
Rwork | 0.170 |
R-free | 0.23524 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | DAA native structure (2DRW) |
RMSD bond length | 0.010 |
RMSD bond angle | 1.255 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.380 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.093 | 0.359 |
Number of reflections | 93589 | |
Completeness [%] | 100.0 | 100 |
Redundancy | 6.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 |