1SMK
Mature and translocatable forms of glyoxysomal malate dehydrogenase have different activities and stabilities but similar crystal structures
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 | 1999-02-10 |
Detector | CUSTOM-MADE |
Wavelength(s) | 1.03321 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 137.430, 88.050, 138.819 |
Unit cell angles | 90.00, 91.53, 90.00 |
Refinement procedure
Resolution | 13.000 - 2.500 |
R-factor | 0.207 |
Rwork | 0.204 |
R-free | 0.25410 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Partially refinend precursor watermelon glyoxysomal malate dehydrogenase |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | EPMR |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 13.000 | 2.660 |
High resolution limit [Å] | 2.500 | 2.500 |
Number of reflections | 98023 | |
Completeness [%] | 85.3 | 88.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4 | 293 | PEG 8000, Sodium Citrate, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |