1H6S
Asymmetric conductivity of engineered proteins
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200B |
| Temperature [K] | 287 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-10-14 |
| Detector | SIEMENS |
| Spacegroup name | H 3 |
| Unit cell lengths | 104.200, 104.200, 124.900 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 36.000 - 3.000 |
| R-factor | 0.197 |
| Rwork | 0.197 |
| R-free | 0.29700 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1prn |
| RMSD bond length | 0.007 |
| RMSD bond angle | 26.470 * |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | CNS |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 36.000 | 3.030 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.081 * | 0.184 * |
| Total number of observations | 66659 * | |
| Number of reflections | 10136 | 1498 * |
| <I/σ(I)> | 19.1 | 5.1 |
| Completeness [%] | 99.0 | 99 |
| Redundancy | 6.6 | 6.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 4.75 * | 50 MM NAOAC PH 4.75, 100 MM (NH4)2SO4, 5.5 % PEG4000 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | 50 (mM) | pH4.75 | |
| 2 | 1 | drop | ammonium sulfate | 100 (mM) | |
| 3 | 1 | drop | PEG4000 | 5.5 (%) | |
| 4 | 1 | drop | octyltetraoxyethylene | 5 (mM) | |
| 5 | 1 | drop | decanoyl sucrose | 12.5 (mM) | |
| 6 | 1 | drop | protein | 5 (mg/ml) |
