1LS1
T. aquaticus Ffh NG Domain at 1.1A Resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-1 |
| Synchrotron site | SSRL |
| Beamline | BL9-1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-04-24 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.98 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 99.734, 53.675, 57.836 |
| Unit cell angles | 90.00, 119.92, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.100 |
| R-factor | 0.13713 |
| Rwork | 0.135 |
| R-free | 0.16900 * |
| Structure solution method | MOLECULAR SUBSTITUTION |
| Starting model (for MR) | 1ffh |
| RMSD bond length | 0.024 * |
| RMSD bond angle | 2.086 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.120 |
| High resolution limit [Å] | 1.100 | 1.100 |
| Rmerge | 0.037 | 0.324 |
| Total number of observations | 694235 * | |
| Number of reflections | 102368 | |
| <I/σ(I)> | 3.2 | |
| Completeness [%] | 95.4 | 89.9 * |
| Redundancy | 4.27 | 2.96 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9 | 295 | PEGMME550, MGCl2, TAPS, pH 9.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 33 (mg/ml) | |
| 2 | 1 | reservoir | PEG550 MME | 30 (%) | |
| 3 | 1 | reservoir | 200 (mM) | ||
| 4 | 1 | reservoir | TAPS | 50 (mM) | pH9.0 |
