2ZAL
Crystal structure of E. coli isoaspartyl aminopeptidase/L-asparaginase in complex with L-aspartate
Replaces: 1SEOExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I711 |
| Synchrotron site | MAX II |
| Beamline | I711 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-04-28 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.095 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 49.890, 77.280, 147.530 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.900 |
| R-factor | 0.158 |
| Rwork | 0.157 |
| R-free | 0.18800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1k2x |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.340 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.064 | 0.256 |
| Number of reflections | 43572 | |
| <I/σ(I)> | 15 | 2.2 |
| Completeness [%] | 95.8 | 91.3 |
| Redundancy | 3.5 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 292 | 100mM Tris/HCl, 80mM calcium chloride, 100mM sodium aspartate, 17% PEG 4000, 13% PEG 400, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K |
