1FJW
THERMOLYSIN (50 MM PHENOL SOAKED)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 298 |
| Detector technology | AREA DETECTOR |
| Collection date | 1998-11-18 |
| Detector | MARRESEARCH |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 93.960, 93.960, 130.915 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 15.000 - 1.900 |
| Rwork | 0.163 |
| R-free | 0.19400 |
| Structure solution method | isomorphous replacement |
| RMSD bond length | 0.014 |
| RMSD bond angle | 0.037 |
| Data reduction software | DENZO |
| Data scaling software | CCP4 ((SCALA)) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.870 |
| Rmerge | 0.090 | 0.380 |
| Number of reflections | 26577 | |
| <I/σ(I)> | 5.7 | 2 |
| Completeness [%] | 93.0 | 93 * |
| Redundancy | 4.2 | 4.2 |
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) |
