1L2F
Crystal structure of NusA from Thermotoga maritima: a structure-based role of the N-terminal domain
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.2 |
Synchrotron site | ALS |
Beamline | 5.0.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-08-01 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.97923,0.97904,0.95372 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 116.191, 116.191, 64.631 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 * - 2.500 |
Rwork | 0.223 |
R-free | 0.29800 |
Structure solution method | MAD, SAD |
RMSD bond length | 0.011 |
RMSD bond angle | 1.580 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.000 | 2.540 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.069 * | 0.434 * |
Number of reflections | 29536 * | 1408 * |
Completeness [%] | 99.8 | 96.8 |
Redundancy | 10.5 * | 8.3 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 295 | ammonium sulfate, PEG400, HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 20 (mM) | pH7.5 |
3 | 1 | drop | EDTA | 1 (mM) | |
4 | 1 | drop | 0.2 (M) | ||
5 | 1 | drop | glycerol | 5 (%) | |
6 | 1 | reservoir | PEG400 | 2 (%) | |
7 | 1 | reservoir | ammonium sulfate | 2.0 (M) | |
8 | 1 | reservoir | HEPES | 0.1 (M) | pH7.5 |