1V6H
The Trimeric Structure Of Divalent Cation Tolerance Protein CutA1 From Thermus Thermophilus HB8
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-D |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2003-07-09 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 71.753, 71.753, 100.399 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 29.200 - 1.900 |
Rwork | 0.188 |
R-free | 0.23400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1nza |
RMSD bond length | 0.006 |
RMSD bond angle | 1.400 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CNS (1.1) |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.990 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.059 | 0.299 |
Number of reflections | 23582 | |
<I/σ(I)> | 17.5 | 6.7 |
Completeness [%] | 97.5 | 90.4 |
Redundancy | 3.4 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.1 | 295 | PEG 20K 16.5% w/w, HEPES 0.1M, 10% w/w of glycerol was added for cryoprotection, pH 6.1, VAPOR DIFFUSION, SITTING DROP, temperature 295K |