1JL1
D10A E. coli ribonuclease HI
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-2 |
Synchrotron site | SSRL |
Beamline | BL9-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-02-28 |
Detector | MARRESEARCH |
Wavelength(s) | 1.000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 37.016, 40.874, 85.305 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.300 |
R-factor | 0.223 * |
Rwork | 0.223 |
R-free | 0.26300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1f21 |
RMSD bond length | 0.008 * |
RMSD bond angle | 2.000 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.360 |
High resolution limit [Å] | 1.300 | 1.300 |
Rmerge | 0.088 | 0.188 * |
Number of reflections | 28054 | |
Completeness [%] | 99.4 | 97.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 295 | used microseeding * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | HEPES | 20 (mM) | pH8.0 |
2 | 1 | reservoir | PEG3350 | 10 (%(w/v)) | |
3 | 1 | drop | protein | 6 (mg/ml) |