1BC5
CHEMOTAXIS RECEPTOR RECOGNITION BY PROTEIN METHYLTRANSFERASE CHER
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 263 |
Detector technology | IMAGE PLATE |
Collection date | 1997-11 |
Detector | RIGAKU |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 65.910, 70.580, 72.790 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.200 |
R-factor | 0.204 |
Rwork | 0.204 |
R-free | 0.28800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1af7 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.690 * |
Data reduction software | DENZO |
Data scaling software | CCP4 |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 23.000 | 2.260 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.064 * | 0.280 * |
Total number of observations | 52170 * | |
Number of reflections | 16682 | |
<I/σ(I)> | 7.8 | 2.6 |
Completeness [%] | 94.5 | 89 |
Redundancy | 3.1 | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 6.8 | PROTEIN WAS CRYSTALLIZED FROM 30 % PEG 5000 MME, 25 MM IMIDAZOLE PH 6.8, 15 MM COCL2, 1MM BETA-MERCAPTOETHANOL. |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 14 (mg/ml) | |
2 | 1 | drop | imidazole | 0.1 (M) | |
3 | 1 | drop | 15 (mM) | ||
4 | 1 | drop | mPEG5000 | 16 (%) | |
5 | 1 | drop | beta-mercaptoethanol | 1 (mM) | |
6 | 1 | reservoir | mPEG5000 | 30 (%) | |
7 | 1 | reservoir | imidazole | 25 (mM) | |
8 | 1 | reservoir | 15 (mM) | ||
9 | 1 | reservoir | beta-mercaptoethanol | 1 (mM) |