3TDC
Crystal Structure of Human Acetyl-CoA carboxylase 2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.1 |
Synchrotron site | ALS |
Beamline | 5.0.1 |
Temperature [K] | 77 |
Detector technology | CCD |
Collection date | 2006-02-13 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.9764 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 113.921, 119.756, 146.035 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.410 |
R-factor | 0.17163 |
Rwork | 0.169 |
R-free | 0.21788 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1uyt |
RMSD bond length | 0.010 |
RMSD bond angle | 1.223 |
Data reduction software | DENZO |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 30.000 |
High resolution limit [Å] | 2.400 |
Rmerge | 0.092 |
Number of reflections | 37827 |
<I/σ(I)> | 19.2 |
Completeness [%] | 96.8 |
Redundancy | 6.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6 | 277 | 6.8% PEG MME 2000, 0.0175M Ammonium Sulfate, 0.1M MES , pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K |