2QRL
Crystal Structure of Oxalylglycine-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 | 2007-05-01 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 64.762, 74.301, 74.619 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.600 |
R-factor | 0.209 |
Rwork | 0.208 |
R-free | 0.24100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2Q99 (BACKBONE ONLY) |
RMSD bond length | 0.013 |
RMSD bond angle | 1.328 |
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] | 29.700 | 29.700 | 1.660 |
High resolution limit [Å] | 1.600 | 3.450 | 1.600 |
Rmerge | 0.056 | 0.029 | 0.358 |
Total number of observations | 34590 | 22894 | |
Number of reflections | 46497 | ||
<I/σ(I)> | 15.8 | 49.3 | 3.5 |
Completeness [%] | 96.5 | 99.3 | 87.6 |
Redundancy | 6.36 | 6.71 | 5.49 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 277 | PEG-MME 2000, Tris, AMP, Oxalylglycine, DTT, pH 8.0, vapor diffusion, hanging drop, temperature 277K |