1EDZ
STRUCTURE OF THE NAD-DEPENDENT 5,10-METHYLENETETRAHYDROFOLATE DEHYDROGENASE FROM SACCHAROMYCES CEREVISIAE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-03-16 |
Detector | RIGAKU RAXIS IV |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 73.980, 73.980, 161.685 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.800 |
R-factor | 0.26 * |
Rwork | 0.260 |
R-free | 0.35000 * |
RMSD bond length | 0.005 |
RMSD bond angle | 1.217 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.092 | 0.263 |
Number of reflections | 10691 * | |
<I/σ(I)> | 12 | |
Completeness [%] | 97.8 | 96.3 |
Redundancy | 4.8 | 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. * |
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) |