1RLK
Structure of Conserved Protein of Unknown Function TA0108 from Thermoplasma acidophilum
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-08-10 |
Detector | SBC-2 |
Wavelength(s) | 0.97915 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 43.456, 43.456, 103.381 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 37.530 - 1.950 |
R-factor | 0.21621 |
Rwork | 0.212 |
R-free | 0.23894 |
Structure solution method | SAD |
RMSD bond length | 0.013 |
RMSD bond angle | 1.154 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SHELXD |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.990 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.058 | 0.405 |
Number of reflections | 8692 | |
<I/σ(I)> | 8.9 | |
Completeness [%] | 99.0 | 98.3 |
Redundancy | 16.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 294 | Calcium chloride, PEG 8000, glycerol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K |