1BH3
E1M, A116K MUTANT OF RH. BLASTICA PORIN
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU FR-C |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1997-07 |
Detector | MARRESEARCH |
Spacegroup name | H 3 |
Unit cell lengths | 104.250, 104.250, 124.930 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.540 - 2.190 |
R-factor | 0.153 * |
Rwork | 0.153 |
R-free | 0.18100 |
Structure solution method | DIFFERENCE FOURIER |
Starting model (for MR) | 1prn |
RMSD bond length | 0.022 |
RMSD bond angle | 0.025 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | CCP4 |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.540 | 2.310 |
High resolution limit [Å] | 2.190 | 2.190 |
Rmerge | 0.056 | 0.223 |
Number of reflections | 25831 | 3665 * |
<I/σ(I)> | 8.8 | 3.3 |
Completeness [%] | 99.3 | 95 * |
Redundancy | 3.7 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.2 | 20 * | Kreusch, A., (1994) J.Mol.Biol., 243, 891. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 20 (mM) | |
3 | 1 | drop | 300 (mM) | ||
4 | 1 | drop | n-octyltetraoxyethylene | 0.6 (%(w/v)) | |
5 | 1 | drop | 3 (mM) | ||
6 | 1 | drop | PEG600 | 10-18 (%) | |
7 | 1 | reservoir | PEG600 | 30-38 (%(w/v)) |