6CQC
RNase P protein from Thermotoga maritima in complex with 1-(4-Fluorophenyl)-2-thiourea
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-11-12 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 0.9785 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 56.136, 64.264, 68.121 |
Unit cell angles | 90.00, 101.63, 90.00 |
Refinement procedure
Resolution | 46.286 - 1.540 |
R-factor | 0.1811 |
Rwork | 0.180 |
R-free | 0.19900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1nz0 |
RMSD bond length | 0.007 |
RMSD bond angle | 0.703 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX ((1.13_2998)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.290 | 1.570 |
High resolution limit [Å] | 1.540 | 1.540 |
Rmerge | 0.044 | 0.237 |
Rmeas | 0.053 | 0.287 |
Rpim | 0.029 | 0.195 |
Number of reflections | 67977 | 2724 |
<I/σ(I)> | 19.5 | 3.7 |
Completeness [%] | 96.9 | 78.5 |
Redundancy | 3.2 | 2.9 |
CC(1/2) | 0.993 | 0.915 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.8 | 292 | P protein from T. maritima in 50 mM Tris-HCl pH 7.5, 0.2 mM EDTA was crystallized at 3 mg/mL in 12% PEG-1000, 100 mm sodium acetate pH 4.8 and 200 mM potassium sulfate |