1EE9
CRYSTAL STRUCTURE OF THE NAD-DEPENDENT 5,10-METHYLENETETRAHYDROFOLATE DEHYDROGENASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH NAD
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-04-09 |
Detector | RIGAKU RAXIS IV |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 73.600, 73.600, 161.601 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 3.000 |
R-factor | 0.25 * |
Rwork | 0.248 |
R-free | 0.36000 |
Structure solution method | DIFFERENCE FOURIER |
RMSD bond length | 0.004 |
RMSD bond angle | 1.216 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 3.000 |
High resolution limit [Å] | 2.900 | 2.900 |
Rmerge | 0.077 | 0.578 |
Number of reflections | 8474 | |
<I/σ(I)> | 11.3 | |
Completeness [%] | 81.3 | 73 |
Redundancy | 3.3 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.2 | 4 * | Monzingo, A.F., (1996) Proteins: Struct., Funct., Genet., 26, 481. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG8000 | 7 (%) | |
2 | 1 | reservoir | Tris-HCl | 50 (mM) |