4PR3
Crystal structure of Brucella melitensis 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL41XU |
Synchrotron site | SPring-8 |
Beamline | BL41XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-02-04 |
Detector | RAYONIX MX225HE |
Wavelength(s) | 0.9791 |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 97.326, 97.326, 175.111 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 37.377 - 2.606 |
R-factor | 0.2262 |
Rwork | 0.222 |
R-free | 0.26240 |
Structure solution method | SAD |
RMSD bond length | 0.004 |
RMSD bond angle | 0.987 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | PHENIX ((phenix.refine: 1.8_1069)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.690 |
High resolution limit [Å] | 2.600 | 2.600 |
Number of reflections | 15654 | |
Completeness [%] | 100.0 | 99.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.2 | 293 | 20%(w/v) PEG-1000, 0.1M phosphate-citrate (pH 4.2), 0.2M Li2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 293K |