2BZG
Crystal structure of thiopurine S-methyltransferase.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-07-14 |
Detector | ADSC CCD |
Spacegroup name | P 42 21 2 |
Unit cell lengths | 85.486, 85.486, 69.362 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 60.410 - 1.580 |
R-factor | 0.214 |
Rwork | 0.213 |
R-free | 0.24900 |
Structure solution method | SAD |
RMSD bond length | 0.020 |
RMSD bond angle | 1.384 |
Data reduction software | d*TREK |
Data scaling software | d*TREK |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 36.390 | 1.640 |
High resolution limit [Å] | 1.580 | 1.580 |
Rmerge | 0.070 | 0.270 |
Number of reflections | 67746 | |
<I/σ(I)> | 11.8 | 4.1 |
Completeness [%] | 99.0 | 92.9 |
Redundancy | 7.09 | 4.24 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | PROTEIN WAS CRYSTALLIZED IN THE PRESENCE OF 6-MERCAPTOPURINE-9-B, D-RIBOFURANOSIDE (PROTEIN: 6-MP-RIBOFURANOSIDE= 1:10) USING THE HANGING DROP VAPOR DIFFUSION METHOD AT 20C BY MIXING 1.5 UL OF THE PROTEIN SOLUTION WITH 1.5 UL OF THE RESERVOIR SOLUTION CONTAINING 24% PEG3350, 0.2 M KCNS, 0.1 M BISTRIS PROPANE, PH 7.0. |