1T3M
Structure of the isoaspartyl peptidase with L-asparaginase activity from E. coli
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 66.318, 71.637, 149.583 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.650 |
| R-factor | 0.1729 |
| Rwork | 0.174 |
| R-free | 0.21670 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ayy |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.025 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AMoRE |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.710 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.010 | 0.528 |
| Number of reflections | 84176 | |
| <I/σ(I)> | 12.1 | 1.97 |
| Completeness [%] | 98.9 | 97.2 |
| Redundancy | 4.7 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 295 | 15% PEG4000, 15% GLYCEROL, 0.3 M MAGNESIUM NITRATE, 0.1 M BIS-TRIS-HCL, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
