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) |






