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) |






