1NOG
Crystal Structure of Conserved Protein 0546 from Thermoplasma Acidophilum
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-02-14 |
Detector | CUSTOM-MADE |
Spacegroup name | P 2 3 |
Unit cell lengths | 89.080, 89.080, 89.080 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.690 - 1.550 |
R-factor | 0.197 |
Rwork | 0.197 |
R-free | 0.21500 |
Structure solution method | MAD |
RMSD bond length | 0.010 |
RMSD bond angle | 0.900 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.600 |
High resolution limit [Å] | 1.550 | 1.550 |
Rmerge | 0.094 * | 0.470 * |
Total number of observations | 341835 * | |
Number of reflections | 62540 * | |
<I/σ(I)> | 21.1 | 4.4 |
Completeness [%] | 99.0 * | 99.8 * |
Redundancy | 10.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 * | 22 * | Christendat, D., (2000) J.Biol.Chem., 275, 24608. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG4000 | 10 (%) | |
2 | 1 | reservoir | sodium acetate | 100 (mM) |