5ET4
Structure of RNase A-K7H/R10H in complex with 3'-CMP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2007-07-06 |
Detector | MAR555 FLAT PANEL |
Wavelength(s) | 0.987 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 160.366, 32.281, 106.963 |
Unit cell angles | 90.00, 125.71, 90.00 |
Refinement procedure
Resolution | 29.125 - 2.100 |
R-factor | 0.2285 |
Rwork | 0.224 |
R-free | 0.32120 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1rpf |
RMSD bond length | 0.009 |
RMSD bond angle | 1.212 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 86.710 | 2.170 |
High resolution limit [Å] | 2.100 | 2.100 |
Number of reflections | 26449 | |
<I/σ(I)> | 10.7 | 3.2 |
Completeness [%] | 99.4 | 99.8 |
Redundancy | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 289 | 800 uL crystallisation condition reservoir formed by 27% PEG4000 and 20 mM sodium cacodylate buffer, pH 5.0. Crystals grew from droplets of 1 uL of protein solution and an equal volume of reservoir solution. |