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 |
