2IV0
Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-07-01 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 81.611, 65.405, 87.181 |
Unit cell angles | 90.00, 95.28, 90.00 |
Refinement procedure
Resolution | 86.710 - 2.500 |
R-factor | 0.199 |
Rwork | 0.196 |
R-free | 0.25400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1v94 |
RMSD bond length | 0.016 |
RMSD bond angle | 1.785 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.640 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.110 | 0.480 |
Number of reflections | 31867 | |
<I/σ(I)> | 11.1 | 3.5 |
Completeness [%] | 99.8 | 100 |
Redundancy | 4.1 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.3 | 0.6M ZNSO4, 0.1M NACACODYLATE, PH6.3, pH 6.30 |