5UBF
Crystal structure of the RctB domains 2-3, RctB-155-483
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 80 |
Detector technology | PIXEL |
Collection date | 2014-07-23 |
Detector | DECTRIS PILATUS 6M-F |
Wavelength(s) | 0.9792 |
Spacegroup name | H 3 |
Unit cell lengths | 128.535, 128.535, 127.775 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 41.966 - 2.600 |
R-factor | 0.2379 |
Rwork | 0.235 |
R-free | 0.27650 |
Structure solution method | SAD |
RMSD bond length | 0.002 |
RMSD bond angle | 0.546 |
Data reduction software | HKL-2000 (v714) |
Data scaling software | HKL-2000 (v714) |
Phasing software | AutoSol (1.11.1-2575-000) |
Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.640 |
High resolution limit [Å] | 2.600 | 2.600 |
Number of reflections | 24150 | |
<I/σ(I)> | 21.73 | |
Completeness [%] | 99.4 | 99 |
Redundancy | 5.7 | 5.4 |
CC(1/2) | 0.506 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 277 | Crystals of selenomethionine-substituted RctB domains 2-3 (155-483) were prepared by mixing 0.1, or 0.2, or 0.4 uL of the protein solution (22.7 mg/ml RctB-155-483 in 20 mM Tris pH 7.4, 500 mM sodium chloride, 5% glycerol, 5 mM 2-mercaptoethanol) and 0.2 uL of reservoir solution (0.1 M Bis-Tris propane pH 6.5, 0.2 M Magnesium chloride, 2% w/v PEG 8000). |