1CHU
STRUCTURE OF L-ASPARTATE OXIDASE: IMPLICATIONS FOR THE SUCCINATE DEHYDROGENASE/ FUMARATE REDUCATSE FAMILY
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1998-03-01 |
| Detector | MARRESEARCH |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 84.750, 84.750, 159.730 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.200 |
| R-factor | 0.225 |
| Rwork | 0.224 |
| R-free | 0.28100 |
| Structure solution method | MIR |
| RMSD bond length | 0.018 |
| RMSD bond angle | 0.045 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | SHARP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.300 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.049 | 0.140 |
| Number of reflections | 33258 | |
| <I/σ(I)> | 9.7 | 2.7 |
| Completeness [%] | 96.9 | 87.4 |
| Redundancy | 3.8 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 * | 22 * | pH 8.3 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 100 (mg/ml) | |
| 2 | 1 | drop | HEPES | 20 (mM) | |
| 3 | 1 | reservoir | PEG4000 | 12-14 (%(w/v)) | |
| 4 | 1 | reservoir | sodium acetate | 100 (mM) | |
| 5 | 1 | reservoir | Tris-HCl | 100 (mM) |
