3SO4
Methionine-adenosyltransferase from Entamoeba histolytica
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL11-1 |
Synchrotron site | SSRL |
Beamline | BL11-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-05-21 |
Wavelength(s) | 0.97945 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 58.492, 113.161, 220.848 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 3.180 |
R-factor | 0.2306 |
Rwork | 0.228 |
R-free | 0.28390 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.203 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | BALBES |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 3.270 |
High resolution limit [Å] | 3.180 | 7.880 | 3.200 |
Rmerge | 0.171 | 0.040 | 0.716 |
Number of reflections | 23472 | ||
<I/σ(I)> | 4.8 | ||
Completeness [%] | 92.2 | 97 | 56 |
Redundancy | 3.8 | 4 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 6.2 | 293 | protein buffer 25 mM HEPES pH 7.5, 500 mM NaCl; crystallization buffer 400 mM Ammonium Acetate, 100 mM BisTris pH 6.2, 33% PEG 3350, vapor diffusion, temperature 293K |