1FJU
THERMOLYSIN (80% ACETONITRILE SOAKED CRYSTALS)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 298 |
| Detector technology | AREA DETECTOR |
| Collection date | 1998-02-03 |
| Detector | MARRESEARCH |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 93.860, 93.860, 131.040 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.000 |
| Rwork | 0.154 |
| R-free | 0.20500 |
| Structure solution method | isomorphous replacement |
| RMSD bond length | 0.013 |
| RMSD bond angle | 0.032 |
| Data reduction software | DENZO |
| Data scaling software | CCP4 ((SCALA)) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.110 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.091 | 0.340 |
| Number of reflections | 22702 | |
| <I/σ(I)> | 6.3 | 2.2 |
| Completeness [%] | 97.0 | 95 |
| Redundancy | 7.3 | 7.5 |
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) |
