2EX4
Crystal Structure of Human methyltransferase AD-003 in complex with S-adenosyl-L-homocysteine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2005-09-13 |
Detector | MARRESEARCH |
Wavelength(s) | 1 |
Spacegroup name | P 1 |
Unit cell lengths | 43.922, 47.367, 64.734 |
Unit cell angles | 105.72, 88.18, 115.97 |
Refinement procedure
Resolution | 62.020 - 1.750 |
R-factor | 0.19731 |
Rwork | 0.194 |
R-free | 0.25789 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1xtp |
RMSD bond length | 0.012 |
RMSD bond angle | 1.345 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 1.790 |
High resolution limit [Å] | 1.750 | 1.750 |
Number of reflections | 41514 | |
Completeness [%] | 92.2 | 92.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 9.5 | 300 | Purified AD-003 was was complexed with S-adenosyl-L-homocysteine (SAH) (Sigma) at 1:5 molar ratio of protein:SAH and crystallized using the hanging drop vapor diffusion method at 20 C by mixing 1.5 l of the protein solution with 1.5 l of the reservoir solution containing 18% PEG 3350, 0.2 M KCl, 0.1 M glycine, pH 9.5., VAPOR DIFFUSION, HANGING DROP, temperature 300K |