4E2G
Crystal structure of Cupin fold protein Sthe2323 from Sphaerobacter thermophilus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-02-02 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97929 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 193.710, 52.623, 108.818 |
Unit cell angles | 90.00, 91.24, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.860 |
R-factor | 0.1614 |
Rwork | 0.159 |
R-free | 0.21110 |
Structure solution method | SAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.132 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.880 |
High resolution limit [Å] | 1.860 | 1.860 |
Rmerge | 0.129 | 0.920 |
Number of reflections | 91471 | |
<I/σ(I)> | 25.38 | 2.01 |
Completeness [%] | 98.9 | 93.6 |
Redundancy | 5.6 | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 289 | 0.2M Ammonium acetate, 0.1M Bis-Tris, 25% PEG3350, 20% glycerol, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |