2O53
Crystal structure of apo-Aspartoacylase from human brain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-10-13 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.033 |
Spacegroup name | P 42 21 2 |
Unit cell lengths | 143.794, 143.794, 104.076 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.700 |
R-factor | 0.21891 |
Rwork | 0.216 |
R-free | 0.26867 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 2o4h |
RMSD bond length | 0.013 |
RMSD bond angle | 1.469 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CCP4 |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.800 |
High resolution limit [Å] | 2.700 | 2.700 |
Number of reflections | 26648 | |
<I/σ(I)> | 17.8 | 2.8 |
Completeness [%] | 87.3 | 47.2 |
Redundancy | 3.9 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | Protein concentration 8-10 mg/ml, 0.05 M Sodium citrate pH 6.0, 0.3 M K2HPO4, 19% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K |