1GTJ
Crystal structure of the thermostable serine-carboxyl type proteinase, kumamolisin (KSCP) - complex with Ac-Ile-Ala-Phe-cho
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 54.760, 78.170, 72.990 |
| Unit cell angles | 90.00, 98.11, 90.00 |
Refinement procedure
| Resolution | 24.870 - 1.780 * |
| R-factor | 0.195 * |
| Rwork | 0.194 |
| R-free | 0.23100 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ga1 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.590 |
| Data reduction software | DENZO |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | CNS (1.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 24.870 | 1.840 |
| High resolution limit [Å] | 1.780 * | 1.780 * |
| Rmerge | 0.041 | 0.202 |
| Total number of observations | 114754 * | |
| Number of reflections | 55533 * | |
| <I/σ(I)> | 10 | 2 |
| Completeness [%] | 97.3 * | 90.6 * |
| Redundancy | 2.1 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 5 * | 20 * | 100 MM SODIUM ACETATE PH 4.5, 400 MM 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 | 0.4 (M) | |
| 5 | 1 | reservoir | sodium acetate | 0.1 (M) | pH4.5 |
