6PRN
E1M, K50A, R52A MUTANT OF RH. BLASTICA PORIN
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1997-08 |
Detector | MARRESEARCH |
Spacegroup name | H 3 |
Unit cell lengths | 104.360, 104.360, 124.250 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.680 - 2.040 |
R-factor | 0.163 * |
Rwork | 0.163 |
R-free | 0.18600 |
Structure solution method | DIFFERENCE FOURIER |
Starting model (for MR) | 1prn |
RMSD bond length | 0.016 |
RMSD bond angle | 0.028 |
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] | 19.700 | 2.150 |
High resolution limit [Å] | 2.040 | 2.040 |
Rmerge | 0.045 | 0.181 |
Number of reflections | 32038 | 4676 * |
<I/σ(I)> | 19.3 | 5.1 |
Completeness [%] | 99.8 | 100 * |
Redundancy | 3.5 | 2.2 |
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)) |