1H66
CRYSTAL STRUCTURE OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE CO WITH 2,5-diaziridinyl-3-hydroxyl-6-methyl-1,4-benzoquinone
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X25 |
Synchrotron site | NSLS |
Beamline | X25 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | BRANDEIS CCD |
Spacegroup name | P 1 |
Unit cell lengths | 56.185, 57.080, 97.323 |
Unit cell angles | 77.05, 77.07, 87.22 |
Refinement procedure
Resolution | 19.960 - 2.000 |
R-factor | 0.199 * |
Rwork | 0.256 |
R-free | 0.25600 * |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 22.100 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.960 | |
High resolution limit [Å] | 2.000 | |
Rmerge | 0.091 * | |
Number of reflections | 73718 | |
Completeness [%] | 93.8 | 83.8 * |
Redundancy | 3.9 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8 * | 25 * | Faig, M., (2000) Proc.Natl.Acad.Sci.USA, 97, 3177. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10-15 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 25 (mM) | |
3 | 1 | drop | FAD | 0.005 (mM) | |
4 | 1 | reservoir | PEG3350 | 30 (%) | |
5 | 1 | reservoir | sodium acetate | 200 (mM) | |
6 | 1 | reservoir | sodium tricine | 100 (mg/ml) | |
7 | 1 | reservoir | FAD | 0.012-0.024 (mM) |