3MPI
Structure of the glutaryl-coenzyme A dehydrogenase glutaryl-CoA complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X10SA |
Synchrotron site | SLS |
Beamline | X10SA |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-11-14 |
Detector | MAR225 |
Wavelength(s) | 0.9999 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 174.990, 114.790, 122.240 |
Unit cell angles | 90.00, 133.95, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.050 |
R-factor | 0.17771 |
Rwork | 0.176 |
R-free | 0.21931 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1siq |
RMSD bond length | 0.012 |
RMSD bond angle | 1.481 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | REFMAC (5.6.0046) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.160 |
High resolution limit [Å] | 2.050 | 2.050 |
Rmerge | 0.058 | 0.519 |
Number of reflections | 100328 | |
<I/σ(I)> | 12.3 | 3.2 |
Completeness [%] | 96.5 | 96.6 |
Redundancy | 3.1 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 277 | 0.01M MES, 0.5M KCL, 10% (w/v) glycerol, 1 mM dithiothreitol, 1 mM FAD, 2 mM glutaryl-CoA, 15% (v,v) MPD, 0.1 M imidazole, pH 6.5, 0.2 M KCl and 2% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 277K |