4R8L
Crystal structure of the Asp-bound guinea pig L-asparaginase 1 catalytic domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-07-31 |
Detector | MARMOSAIC 300 mm CCD |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 123.210, 156.000, 158.820 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.961 - 2.410 |
R-factor | 0.20727 |
Rwork | 0.206 |
R-free | 0.23612 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.368 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0071) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 111.290 | 2.550 |
High resolution limit [Å] | 2.410 | 2.410 |
Number of reflections | 58821 | |
Completeness [%] | 98.7 | 96.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 0.1 M HEPES, 15% PEG 4000, 10 mM L-aspartic acid sodium salt monohydrate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |