2HLS
The crystal structure of a protein disulfide oxidoreductase from Aeropyrum pernix k1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ELETTRA BEAMLINE 5.2R |
Synchrotron site | ELETTRA |
Beamline | 5.2R |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-12-14 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 1.2 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 90.625, 101.424, 128.927 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.930 |
Rwork | 0.187 |
R-free | 0.20900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ayt |
RMSD bond length | 0.005 |
RMSD bond angle | 1.200 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.000 |
High resolution limit [Å] | 1.930 | 1.930 |
Number of reflections | 44495 | |
<I/σ(I)> | 36.9 | 2.9 |
Completeness [%] | 98.1 | 87.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | 2M ammonium sulfate, 2% PEG 400, 0.1M HEPES, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 298K |