1NDB
Crystal structure of Carnitine Acetyltransferase
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 | 2002-08-23 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9790 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 158.884, 89.654, 119.436 |
Unit cell angles | 90.00, 127.46, 90.00 |
Refinement procedure
Resolution | 30.000 * - 1.800 |
R-factor | 0.1921 |
Rwork | 0.192 |
R-free | 0.21700 * |
Structure solution method | SAD |
RMSD bond length | 0.005 |
RMSD bond angle | 21.500 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SnB |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.910 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.044 * | 0.120 * |
Total number of observations | 749015 * | |
Number of reflections | 235313 | |
Completeness [%] | 97.0 | 94 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 4 * | 100mM TRIS, 20% PEG 3350, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | Tris | 100 (mM) | pH7.5 |
2 | 1 | reservoir | PEG3350 | 20 (%(w/v)) | |
3 | 1 | drop | protein | 20 (mg/ml) |