1NG1
N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE RECOGNITION PROTEIN FFH FROM THERMUS AQUATICUS
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL7-1 |
| Synchrotron site | SSRL |
| Beamline | BL7-1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-07-04 |
| Detector | MARRESEARCH |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 100.072, 100.072, 73.490 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.030 |
| R-factor | 0.189 |
| Rwork | 0.189 |
| R-free | 0.25000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ffh |
| RMSD bond length | 0.013 |
| RMSD bond angle | 22.680 * |
| Data reduction software | SOFTWARE (AT SYNCHROTRON) |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR (3.851) |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.100 |
| High resolution limit [Å] | 2.030 | 2.030 |
| Rmerge | 0.089 | 0.396 |
| Number of reflections | 24684 | |
| <I/σ(I)> | 18.2 | 4.7 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 8 | 7.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 6.5 | pH 6.50 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 13 (mg/ml) | |
| 2 | 1 | drop | GDP | 1.2 (mM) | |
| 3 | 1 | drop | 5 (mM) | ||
| 4 | 1 | reservoir | PEG8000 | 10 (%(w/v)) | |
| 5 | 1 | reservoir | sodium cacodylate | 0.1 (M) | |
| 6 | 1 | reservoir | magnesium acetate | 0.2 (M) |
