1KY5
D244E mutant S-Adenosylhomocysteine hydrolase refined with noncrystallographic restraints
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 93 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-01-01 |
| Detector | RIGAKU RAXIS IIC |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 91.000, 223.000, 91.200 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.800 |
| R-factor | 0.2155 |
| Rwork | 0.215 |
| R-free | 0.28700 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 27.000 * |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.920 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.070 | 0.140 |
| Number of reflections | 43000 | |
| <I/σ(I)> | 11 | 5 |
| Completeness [%] | 98.0 | 83 |
| Redundancy | 6 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 22 * | used seeding, Komoto, J., (2000) J.Biol.Chem., 275, 32147. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG4000 | 15 (%(w/v)) | |
| 2 | 1 | reservoir | Tris-HCl | 50 (mM) | |
| 3 | 1 | reservoir | glycerol | 2 (%(v/v)) | |
| 4 | 1 | reservoir | isopropanol | 5 (%(v/v)) | |
| 5 | 1 | reservoir | dithiothreitol | 1 (mM) | |
| 6 | 1 | drop | protein | 10 (mg/ml) |
