1JXB
I53A, a point mutant of the cysteine-free variant of E. coli Rnase HI
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.2 |
Synchrotron site | ALS |
Beamline | 5.0.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-12-19 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 36.867, 40.830, 85.016 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 12.500 - 1.600 |
R-factor | 0.207 * |
Rwork | 0.207 |
R-free | 0.25700 |
Structure solution method | MOLECULAR REPLACEMENT |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 1.660 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.062 * | |
Number of reflections | 34997 | |
Completeness [%] | 95.2 | 91.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | used microseeding * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | HEPES | 20 (mM) | pH7.5 |
2 | 1 | drop | PEG3350 | 10 (%) | |
3 | 1 | drop | protein | 4 (mg/ml) |