Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 90 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-05 |
| Detector | MARRESEARCH |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 60.840, 60.840, 207.910 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 9.000 - 2.138 |
| R-factor | 0.2 * |
| Rwork | 0.199 |
| R-free | 0.25700 |
| Structure solution method | OTHER |
| RMSD bond length | 0.011 |
| RMSD bond angle | 0.027 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 2.180 |
| High resolution limit [Å] | 2.138 | 2.130 |
| Rmerge | 0.069 | 0.236 |
| Total number of observations | 63933 * | |
| Number of reflections | 12963 | |
| <I/σ(I)> | 13 | |
| Completeness [%] | 96.3 | 64.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 5.4 | 4 * | Dattagupta, J.K., (1999) Proteins: Struct., Funct., Genet., 35, 321 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 8.6 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 71.4 (mM) | |
| 3 | 1 | drop | 286 (mM) | ||
| 4 | 1 | drop | ammonium sulfate | 1.4 (%) | |
| 5 | 1 | drop | sodium acetate | 2.9 (mM) | |
| 6 | 1 | reservoir | ammonium sulfate | 25 (%) | |
| 7 | 1 | reservoir | sodium acetate | 10 (mM) |
