2I9C
Crystal Structure of the Protein RPA1889 from Rhodopseudomonas palustris CGA009
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-BM |
Synchrotron site | APS |
Beamline | 19-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-06-09 |
Detector | SBC-3 |
Wavelength(s) | 0.97904 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 78.022, 78.022, 38.979 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 33.790 - 2.000 |
R-factor | 0.17603 |
Rwork | 0.175 |
R-free | 0.20189 |
Structure solution method | SAD |
RMSD bond length | 0.020 |
RMSD bond angle | 1.605 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 67.570 | 2.020 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.066 | 0.299 |
Number of reflections | 9449 | |
<I/σ(I)> | 6.83 | |
Completeness [%] | 99.7 | 100 |
Redundancy | 7 | 7.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 5% Tascimate, 10% PEG5000 MME, 0.1M HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |