1PEG
Structural basis for the product specificity of histone lysine methyltransferases
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-11-22 |
| Detector | ADSC QUANTUM 315 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 68.260, 94.170, 114.690 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.000 * - 2.590 |
| R-factor | 0.22 |
| Rwork | 0.220 |
| R-free | 0.32000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ml9 |
| RMSD bond length | 0.009 * |
| RMSD bond angle | 1.600 * |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.000 | 2.680 |
| High resolution limit [Å] | 2.590 | 2.590 |
| Rmerge | 0.088 | 0.228 |
| Number of reflections | 21803 | 1578 * |
| <I/σ(I)> | 23.3 | 4.5 |
| Completeness [%] | 91.6 | 67.6 |
| Redundancy | 4.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 9.8 * | 16 * | PEG 2000 monomethyl ether, trimethylamine, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 289K, pH 8.40 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 12 (mg/ml) | |
| 10 | 1 | reservoir | dithiothreitol | 5 (mM) | |
| 2 | 1 | drop | glycine | 20 (mM) | pH9.8 |
| 3 | 1 | drop | 150 (mM) | ||
| 4 | 1 | drop | dithiothreitol | 5 (mM) | |
| 5 | 1 | drop | glycerol | 5 (%) | |
| 6 | 1 | drop | AdoHcy | 600000 (nM) | |
| 7 | 1 | reservoir | Tris | 0.1 (M) | pH8.4-8.6 |
| 8 | 1 | reservoir | PEG2000 MME | 20-25 (%) | |
| 9 | 1 | reservoir | trimethylamine | 0.2 (M) |
