1J9A
OLIGORIBONUCLEASE
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 115 |
Detector technology | CCD |
Collection date | 2000-02-27 |
Detector | BRUKER |
Wavelength(s) | 0.9794, 0.9796, 0.9641, 0.9832 |
Spacegroup name | P 41 2 2 |
Unit cell lengths | 55.110, 55.110, 144.430 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.500 |
R-factor | 0.1851 |
R-free | 0.29860 |
RMSD bond length | 0.006 |
RMSD bond angle | 0.026 |
Data reduction software | HKL-2000 |
Phasing software | SHELX |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.600 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.040 | 0.150 |
Number of reflections | 14507 | |
<I/σ(I)> | 15 | 2 |
Completeness [%] | 100.0 | 100 |
Redundancy | 4 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.3 | Protein solution: 15 mg/mL protein in 0.01 M HEPES, 0.15 M sodium chloride, 0.005 M DTT, 0.005 M EDTA with pH 7.1-8.0. Reservoir: 2.3 M ammonium sulfate at pH 7.1-7.5. Hanging drop vapor diffusion method. Drops were formed by combining 4 microliters reservoir solution with 4 microliters protein solution. Room temperature., pH 7.3 |