1KY2
GPPNHP-BOUND YPT7P AT 1.6 A RESOLUTION
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-11-10 |
Detector | MARRESEARCH |
Wavelength(s) | 0.934 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 40.137, 60.667, 73.537 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 - 1.600 |
R-factor | 0.183 * |
Rwork | 0.183 |
R-free | 0.23900 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ek0 |
RMSD bond length | 0.008 * |
RMSD bond angle | 1.824 * |
Data scaling software | XDS |
Phasing software | AMoRE |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 1.700 |
High resolution limit [Å] | 1.600 | 1.570 * |
Rmerge | 0.103 * | 0.181 * |
Total number of observations | 124357 * | |
Number of reflections | 23450 | |
<I/σ(I)> | 8.1 | 2.7 |
Completeness [%] | 96.2 | 95.7 |
Redundancy | 5.15 | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 20 * | PEG, TRIS, GppNHp, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 7-9 (mg/ml) | |
2 | 1 | reservoir | 1 (M) | ||
3 | 1 | reservoir | PEG6000 | 20-30 (%) |