3C17
Hexagonal 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 | 2007-02-03 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 149.470, 149.470, 214.350 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 44.510 - 1.950 |
| R-factor | 0.184 |
| Rwork | 0.184 |
| R-free | 0.20300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1k2x |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.399 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.670 | 2.060 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.107 | 0.760 |
| Number of reflections | 98405 | |
| <I/σ(I)> | 14.3 | 2.2 |
| Completeness [%] | 96.6 | 98.5 |
| Redundancy | 5.9 | 5.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 292 | 4.3M NaCl, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K |
