4G24
Crystal Structure of proteinaceous RNase P 1 (PRORP1) from A. thaliana with Mn
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-03-23 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.968 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 41.750, 112.475, 138.762 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 36.190 - 1.950 |
R-factor | 0.19552 |
Rwork | 0.194 |
R-free | 0.22654 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.011 |
RMSD bond angle | 1.380 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.020 |
High resolution limit [Å] | 1.950 | 1.950 |
Number of reflections | 48526 | |
<I/σ(I)> | 16 | 3.9 |
Completeness [%] | 99.9 | 100 |
Redundancy | 6.2 | 6.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 277 | 18% PEG 3350, 0.1 M sodium citrate tribasic pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K |