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 |