2ZAK
Orthorhombic crystal structure of precursor E. coli isoaspartyl peptidase/L-asparaginase (EcAIII) with active-site T179A mutation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X12 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X12 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-02-02 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1.000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.350, 77.780, 147.930 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 - 2.010 |
R-factor | 0.19961 |
Rwork | 0.197 |
R-free | 0.25285 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1k2x |
RMSD bond length | 0.016 |
RMSD bond angle | 1.548 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.103 | 0.400 |
Number of reflections | 38010 | |
<I/σ(I)> | 9.2 | 2.1 |
Completeness [%] | 94.0 | 69.1 |
Redundancy | 3 | 2.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 292 | 200mM MgCl2, 100mM Tris/HCl, 15% PEG 4000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K |