1SFN
Crystal structure of protein DR1152 from Deinococcus radiodurans R1, Pfam DUF861
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X9A |
Synchrotron site | NSLS |
Beamline | X9A |
Temperature [K] | 110 |
Detector technology | CCD |
Collection date | 2004-01-16 |
Detector | MARRESEARCH |
Wavelength(s) | 1.01 |
Spacegroup name | P 4 21 2 |
Unit cell lengths | 109.370, 109.370, 95.408 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 - 2.460 |
R-factor | 0.281 |
Rwork | 0.229 |
R-free | 0.27800 |
Structure solution method | SAD |
RMSD bond length | 0.007 |
RMSD bond angle | 1.520 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.550 |
High resolution limit [Å] | 2.460 | 2.460 |
Rmerge | 0.042 | 0.144 |
Number of reflections | 21111 | |
<I/σ(I)> | 48.1 | 10.5 |
Completeness [%] | 97.8 | 94.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | Maleic acid, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |