1HG1
X-ray structure of the complex between Erwinia chrysanthemi L-asparaginase and D-aspartate
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X9B |
Synchrotron site | NSLS |
Beamline | X9B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-11-15 |
Detector | ADSC CCD |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 105.840, 90.425, 126.893 |
Unit cell angles | 90.00, 91.80, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.800 |
R-factor | 0.179 |
Rwork | 0.179 |
R-free | 0.20400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PREVIUOSLY PUBLISHED STRUCTURE OF ERWINIA CHRYSANTHEMI L-ASPARAGINSE (MILLER ET AL. FEBS LETT. 1993 |
RMSD bond length | 0.005 |
RMSD bond angle | 23.020 * |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.082 * | 0.530 * |
Total number of observations | 331851 * | |
Number of reflections | 100021 | |
<I/σ(I)> | 7.4 | 2.1 |
Completeness [%] | 90.1 | 74.7 |
Redundancy | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 5.4 | Miller, M., (1993) FEBS Lett., 328, 275. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | ammonium sulfate | 50 (%) | |
2 | 1 | reservoir | CHES | 0.1 (M) | |
3 | 1 | reservoir | PEG400 | 2 (%(w/v)) |