1GTG
Crystal structure of the thermostable serine-carboxyl type proteinase, kumamolysin (kscp)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 42.630, 78.320, 49.000 |
| Unit cell angles | 90.00, 106.33, 90.00 |
Refinement procedure
| Resolution | 36.300 * - 2.270* |
| R-factor | 0.206 * |
| Rwork | 0.206 |
| R-free | 0.25800 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ga1 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.650 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | CNS (1.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 36.300 * | 2.390 |
| High resolution limit [Å] | 2.270 * | 2.270 |
| Rmerge | 0.091 * | 0.232 |
| Total number of observations | 26014 * | |
| Number of reflections | 13692 * | |
| <I/σ(I)> | 7 | 3.1 |
| Completeness [%] | 95.6 | 87.4 * |
| Redundancy | 1.9 | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 5 * | 20 * | 100 MM SODIUM ACETATE PH 5.2 1.2 M AMMONIUM SULPHATE |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 9 (mg/ml) | |
| 2 | 1 | drop | 25 (mM) | ||
| 3 | 1 | drop | sodium acetate | 50 (mM) | pH5. |
| 4 | 1 | reservoir | ammonium sulfate | 1.2 (M) | |
| 5 | 1 | reservoir | sodium acetate | 0.1 (M) | pH5.2 |
