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 |