1K62
Crystal Structure of the Human Argininosuccinate Lyase Q286R Mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 298 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-10-15 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 104.202, 104.202, 183.019 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 17.000 * - 2.650 |
| R-factor | 0.175 |
| Rwork | 0.175 |
| R-free | 0.23000 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1auw |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.100 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 17.000 | 2.740 |
| High resolution limit [Å] | 2.650 | 2.650 |
| Rmerge | 0.100 * | 0.460 * |
| Total number of observations | 79294 * | |
| Number of reflections | 33242 * | |
| <I/σ(I)> | 8.1 | |
| Completeness [%] | 97.8 | 99.2 |
| Redundancy | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.1 * | 298 | Turner, M.A., (1997) Proc.Natl.Acad.Sci.USA, 94, 9063. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10-15 (mg/ml) | |
| 2 | 1 | drop | phosphate | 50 (mM) | |
| 3 | 1 | drop | dithiothreitol | 5 (mM) | |
| 4 | 1 | reservoir | phosphate | 1.1 (M) |
