4E2Q
Crystal Structure of (S)-Ureidoglycine Aminohydrolase from Arabidopsis thaliana
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 4A |
Synchrotron site | PAL/PLS |
Beamline | 4A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-07-26 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97973 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 93.856, 175.773, 155.176 |
Unit cell angles | 90.00, 99.39, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.500 |
Rwork | 0.224 |
R-free | 0.28600 |
Structure solution method | SAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.490 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX (AUTOMR) |
Refinement software | CNS (1.21) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.564 | |
Number of reflections | 137345 | |
<I/σ(I)> | 2.6 | |
Completeness [%] | 94.6 | |
Redundancy | 6.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 295 | 0.1M HEPES, 7% (w/v) PEG 8000, 8% (w/v) ethylene glycol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |