5GVY
Crystal structure of SALT protein from Oryza sativa
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2016-07-22 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 48.291, 58.811, 51.558 |
Unit cell angles | 90.00, 114.39, 90.00 |
Refinement procedure
Resolution | 25.555 - 1.662 |
R-factor | 0.1641 |
Rwork | 0.162 |
R-free | 0.20050 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1c3m |
RMSD bond length | 0.007 |
RMSD bond angle | 0.912 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AutoSol |
Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.690 |
High resolution limit [Å] | 1.660 | 1.660 |
Rmerge | 0.033 | 0.134 |
Number of reflections | 31076 | |
<I/σ(I)> | 35.8 | 6.071 |
Completeness [%] | 97.4 | 76.8 |
Redundancy | 2.5 | 1.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 291 | Protein buffer-10mM Sodium phosphate, 1.8mM Potassium phosphate, 137mM NaCl, 2.7mM KCl. Crystallization buffer-200mM NaCl, 100mM Tris pH 8.8, 25% w/v PEG 3350 |