1P0Y
Crystal structure of the SET domain of LSMT bound to MeLysine and AdoHcy
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 95 |
Detector technology | IMAGE PLATE |
Collection date | 2003-01-25 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 130.410, 153.190, 266.320 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 * - 2.550 |
R-factor | 0.228 |
Rwork | 0.228 |
R-free | 0.26900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1mlv |
RMSD bond length | 0.007 |
RMSD bond angle | 21.300 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS (1.1) |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.640 |
High resolution limit [Å] | 2.550 | 2.550 |
Rmerge | 0.044 * | 0.485 * |
Number of reflections | 83829 | 7768 * |
<I/σ(I)> | 30.2 | 2.45 |
Completeness [%] | 96.5 | 93.6 |
Redundancy | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.8 | 25 * | 0.95-1.10 M Sodium Acetate, 100 mM Methyllysine Acetate, 1 mM TCEP, 400 uM S-adenosylhomocysteine, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | sodium acetate | 0.95-1.10 (M) | |
3 | 1 | reservoir | AdoHcy | 4000 (nM) | |
4 | 1 | reservoir | TCEP | 1 (mM) | |
5 | 1 | reservoir | Lys | 100 (mM) | or MeLys, pH6.8 |