1LT3
HEAT-LABILE ENTEROTOXIN DOUBLE MUTANT N40C/G166C
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 295 |
Detector technology | IMAGE PLATE |
Collection date | 1996-09 |
Detector | RIGAKU RAXIS IV |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 119.700, 101.100, 64.200 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.000 |
R-factor | 0.188 |
Rwork | 0.188 |
R-free | 0.26100 |
Structure solution method | ISOMORPHOUS MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ltt |
RMSD bond length | 0.011 |
RMSD bond angle | 23.100 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.053 * | 0.175 * |
Number of reflections | 48385 | |
<I/σ(I)> | 17 | 4.5 |
Completeness [%] | 90.5 | 72.3 * |
Redundancy | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | three-layer capillary method * | 7.5 | PROTEIN WAS CRYSTALLIZED FROM 5% PEG 6000, 100 MM NACL, 1 MM EDTA, 75 MM LACTOSE, 100 MM TRIS PH 7.5 USING THE 3 LAYER CAPPILARY METHOD, 3 layer capillary method |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | LT-I N40C/G166C | 5 (mg/ml) | |
2 | 1 | 2 | PEG6000 | 5.6 (%) | |
3 | 1 | 2 | Tris-HCl | 100 (mM) | |
4 | 1 | 2 | 100 (mM) | 2 | |
5 | 1 | 2 | 0.02 (%) | ||
6 | 1 | 2 | lactose | 75 (mM) | |
7 | 1 | 2 | guanyltyramine | 1.5 (mM) |