2A0B
HISTIDINE-CONTAINING PHOSPHOTRANSFER DOMAIN OF ARCB FROM ESCHERICHIA COLI
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 277 |
Detector technology | IMAGE PLATE |
Collection date | 1997-09 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 30.456, 34.924, 110.741 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 6.000 - 1.570 |
Rwork | 0.190 |
R-free | 0.24500 |
RMSD bond length | 0.024 |
RMSD bond angle | 0.036 |
Data reduction software | PROCESS |
Data scaling software | PROCESS |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 1.700 | |
High resolution limit [Å] | 1.570 | 1.570 |
Rmerge | 0.049 | 0.190 |
Total number of observations | 98202 * | |
Number of reflections | 16338 | |
<I/σ(I)> | 66 | |
Completeness [%] | 95.0 * | 89 |
Redundancy | 6 | 5.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 4.1 | 277 * | PROTEIN WAS CRYSTALLIZED FROM 12.5% PEGMME 550, 5 MM ZNSO4, 50 MM ACETIC ACID/SODIUM ACETATE BUFFER, PH 4.1 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10.6 (mg/ml) | |
2 | 1 | drop | acetic acid/sodium acetate | 50 (mM) | |
3 | 1 | drop | 5 (mM) | ||
4 | 1 | drop | mPEG550 | 12.5 (%) | |
5 | 1 | reservoir | mPEG550 | 13 (%) |