4O0C
High resolution crystal structure of uncleaved human L-asparaginase protein
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 | 2013-08-18 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97856 |
Spacegroup name | P 65 |
Unit cell lengths | 59.213, 59.213, 297.793 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 29.040 - 1.500 |
R-factor | 0.15465 |
Rwork | 0.152 |
R-free | 0.20529 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4GDV |
RMSD bond length | 0.012 |
RMSD bond angle | 1.559 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.590 |
High resolution limit [Å] | 1.500 | 1.500 |
Number of reflections | 92426 | |
<I/σ(I)> | 13.2 | 2.86 |
Completeness [%] | 99.0 | 94.3 |
Redundancy | 8.1 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 2.2-2.5 M sodium Malonate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |