5ELL
Crystal structure of L-aspartate/glutamate-specific racemase from Escherichia coli
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 7A (6B, 6C1) |
Synchrotron site | PAL/PLS |
Beamline | 7A (6B, 6C1) |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-12-22 |
Detector | ADSC QUANTUM 270 |
Wavelength(s) | 0.987 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 82.172, 147.859, 82.182 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.687 - 1.801 |
R-factor | 0.166 |
Rwork | 0.164 |
R-free | 0.20160 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1jfl |
RMSD bond length | 0.007 |
RMSD bond angle | 0.950 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.830 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.324 | |
Number of reflections | 46553 | |
<I/σ(I)> | 23.53 | 3.44 |
Completeness [%] | 96.3 | 90.8 |
Redundancy | 4.8 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 0.3 M ammonium nitrate, 14~16% PEG 3350 |