1EFL
HUMAN MALIC ENZYME IN A QUATERNARY COMPLEX WITH NAD, MG, AND TARTRONATE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X4A |
Synchrotron site | NSLS |
Beamline | X4A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-09-11 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 228.800, 117.000, 114.300 |
Unit cell angles | 90.00, 109.20, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.600 |
R-factor | 0.206 |
Rwork | 0.206 |
R-free | 0.28500 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.400 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | GLRF |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.700 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.070 | 0.204 |
Number of reflections | 81974 | |
<I/σ(I)> | 12 | |
Completeness [%] | 94.0 | 88 |
Redundancy | 2.5 | 1.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.4 * | 4 * | 100 mM MES, 8% PEG20000, 5% MPD, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 8 (mg/ml) | |
10 | 1 | reservoir | MES | 100 (mM) | |
11 | 1 | reservoir | PEG20000 | 6-11 (%) | |
12 | 1 | reservoir | MPD | 5 (%(v/v)) | |
2 | 1 | drop | Tris-HCl | 30 (mM) | |
3 | 1 | drop | 80 (mM) | ||
4 | 1 | drop | dithiothreitol | 4 (mM) | |
5 | 1 | drop | EDTA | 0.1 (mM) | |
6 | 1 | drop | NAD+ | 0.4-1.2 (mM) | |
7 | 1 | drop | 5-10 (mM) | ||
8 | 1 | drop | fumarate | 5 (mM) | |
9 | 1 | drop | tatronate | 5 (mM) |