4LVE
LEN K30T MUTANT: A DOMAIN FLIP AS A RESULT OF A SINGLE AMINO ACID SUBSTITUTION
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 120 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-02 |
| Detector | RIGAKU |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 46.200, 54.600, 91.400 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.300 |
| R-factor | 0.19 |
| Rwork | 0.190 |
| R-free | 0.26700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | DIMER GENERATED FROM 3LVE |
| RMSD bond length | 0.006 |
| RMSD bond angle | 25.700 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (0.3C) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.059 | 0.219 |
| Number of reflections | 16282 | |
| <I/σ(I)> | 18 | 5.3 |
| Completeness [%] | 93.2 | 81.6 |
| Redundancy | 7.4 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 7.5 | pH 7.5 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 8.5 (mg/ml) | |
| 2 | 1 | drop | ammonium sulfate | 1.8 (M) | |
| 3 | 1 | drop | HEPES | 0.1 (M) |
