1FJO
THERMOLYSIN (60% ACETONE SOAKED CRYSTALS)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 298 |
| Detector technology | AREA DETECTOR |
| Collection date | 1998-02-12 |
| Detector | MARRESEARCH |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 94.080, 94.080, 131.240 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 15.000 - 2.000 |
| Rwork | 0.156 |
| R-free | 0.20700 |
| Structure solution method | isomorphous replacement |
| RMSD bond length | 0.013 |
| RMSD bond angle | 0.034 |
| Data reduction software | DENZO |
| Data scaling software | CCP4 ((SCALA)) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 2.110 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.082 | 0.164 |
| Number of reflections | 22715 | |
| <I/σ(I)> | 6.1 | |
| Completeness [%] | 96.0 | 94 |
| Redundancy | 5.9 | 6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 7.5 | 298 | English, A.C., (1999) Proteins Struct.Funct.Genet., 37, 628. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 4.6 (mM) | |
| 2 | 1 | 1 | DMSO | 45 (%) | |
| 3 | 1 | 1 | Tris-HCl | 50 (mm) | |
| 4 | 1 | 1 | 2.5 (M) |
