1CM7
3-ISOPROPYLMALATE DEHYDROGENASE FROM ESCHERICHIA COLI
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 277 |
Detector technology | IMAGE PLATE |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 55.800, 86.900, 83.700 |
Unit cell angles | 90.00, 93.30, 90.00 |
Refinement procedure
Resolution | 6.000 - 2.060 |
Rwork | 0.173 |
R-free | 0.24500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1 IPD |
RMSD bond length | 0.010 |
RMSD bond angle | 1.700 |
Phasing software | AMoRE |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.060 |
Rmerge | 0.058 * |
Total number of observations | 89369 * |
Number of reflections | 36432 |
Completeness [%] | 79.0 * |
Redundancy | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | 15 MG/ML PROTEIN IN 15% PEG 4K, 50 MM TRIS PH = 7.5, 0.35 M MGCL2 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | reservoir | PEG4000 | 15 (%(w/v)) | |
3 | 1 | reservoir | Tris-HCl | 50 (mM) | |
4 | 1 | reservoir | 0.35 (M) |