1JCT
Glucarate Dehydratase, N341L mutant Orthorhombic Form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-BM |
Synchrotron site | APS |
Beamline | 19-BM |
Temperature [K] | 113 |
Detector technology | CCD |
Collection date | 2000-06-23 |
Detector | CUSTOM-MADE |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 73.924, 203.159, 136.185 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.750 |
R-factor | 0.213 * |
Rwork | 0.213 |
R-free | 0.27400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ec8 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.300 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.850 |
High resolution limit [Å] | 2.750 | 2.750 |
Rmerge | 0.071 | 0.394 |
Total number of observations | 100153 * | |
Number of reflections | 24649 | |
<I/σ(I)> | 10.5 | |
Completeness [%] | 91.1 | 93.5 |
Redundancy | 4.1 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 8 | 4 * | used macroseeding * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | Tris-HCl | 10 (mM) | pH8.0 |
2 | 1 | 1 | 5 (mM) | ||
3 | 1 | 1 | protein | 14.5 (mg/ml) | |
4 | 1 | 2 | mPEG5000 | 14 (%) | |
5 | 1 | 2 | 50 (mM) | ||
6 | 1 | 2 | 2-propanol | 5 (%) | pH8.0 |
7 | 1 | 2 | HEPPS | 5 (%) |