1FFH
N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE RECOGNITION PROTEIN FFH FROM THERMUS AQUATICUS
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1996-03-19 |
Detector | MAR scanner 300 mm plate |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 99.900, 53.910, 57.360 |
Unit cell angles | 90.00, 119.77, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.050 |
R-factor | 0.186 |
Rwork | 0.186 |
R-free | 0.24800 |
Structure solution method | MIR |
RMSD bond length | 0.006 |
RMSD bond angle | 21.320 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.843) |
Refinement software | X-PLOR (3.843) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 2.120 | |
High resolution limit [Å] | 2.050 | 2.050 |
Rmerge | 0.046 * | 0.137 * |
Number of reflections | 16644 | |
Completeness [%] | 99.5 | 98.4 |
Redundancy | 4 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9 | PROTEIN AT 30 MG/ML IN WATER. CRYSTALLIZED AT RT BY SITTING DROP VAPOR DIFFUSION USING 30% PEG MME 550, 50 MM TAPS PH 9.0, 200 MM MGCL2., vapor diffusion - sitting drop |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 30 (mg/ml) | |
2 | 1 | reservoir | mPEG550 | 30 (%) | |
3 | 1 | reservoir | TAPS | 100 (mM) | |
4 | 1 | reservoir | 200 (mM) |