2QRK
Crystal Structure of AMP-bound Saccharopine Dehydrogenase (L-Lys Forming) from Saccharomyces cerevisiae
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH3R |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2007-03-14 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.970, 69.106, 127.829 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.750 |
| R-factor | 0.2 |
| Rwork | 0.199 |
| R-free | 0.23300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2Q99 (BACKBONE ONLY) |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.412 |
| Data reduction software | d*TREK |
| Data scaling software | d*TREK (9.6D) |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 29.010 | 29.010 | 1.810 |
| High resolution limit [Å] | 1.750 | 3.770 | 1.750 |
| Rmerge | 0.034 | 0.020 | 0.154 |
| Total number of observations | 26782 | 19314 | |
| Number of reflections | 41009 | ||
| <I/σ(I)> | 25.9 | 63.4 | 8.8 |
| Completeness [%] | 97.8 | 98.6 | 91.9 |
| Redundancy | 5.87 | 5.96 | 5.06 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277 | PEG-MME 2000, Bis-Tris, AMP, pH 6.5, vapor diffusion, hanging drop, temperature 277K |






