2JDX
CRYSTAL STRUCTURE OF HUMAN L-ARGININE:GLYCINE AMIDINOTRANSFERASE, DELETIONMUTANT ATDELTAM302
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 83.710, 83.710, 200.410 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.900 |
| R-factor | 0.173 |
| Rwork | 0.173 |
| Structure solution method | OTHER |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.570 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((AGROVATA) |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | |
| High resolution limit [Å] | 2.900 | |
| Rmerge | 0.104 * | 0.365 * |
| Total number of observations | 73369 * | |
| Number of reflections | 16068 * | |
| Completeness [%] | 97.7 | 99.8 * |
| Redundancy | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7 | drop was made of a 7 micro litter protein solution and 14 micro litter of a reservoir solution * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 13 (mg/ml) | |
| 2 | 1 | drop | HEPES-NaOH | 30 (mM) | |
| 3 | 1 | drop | EDTA | 0.5 (mM) | |
| 4 | 1 | drop | GSH | 0.5 (mM) | |
| 5 | 1 | reservoir | PEG6000 | 3 (%(w/v)) | |
| 6 | 1 | reservoir | HEPES-NaOH | 40 (mM) |
