1R8B
Crystal Structures of an Archaeal Class I CCA-Adding Enzyme and Its Nucleotide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X26C |
Synchrotron site | NSLS |
Beamline | X26C |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.0 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 86.402, 79.371, 78.135 |
Unit cell angles | 90.00, 97.33, 90.00 |
Refinement procedure
Resolution | 38.630 - 2.000 |
R-factor | 0.18315 |
Rwork | 0.181 |
R-free | 0.22600 * |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.016 |
RMSD bond angle | 1.447 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.068 * | |
Number of reflections | 35218 | |
Completeness [%] | 99.9 * | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 6.4 | 293 | Calcium Chloride, Ethanol, Tris, magnesium chloride, sodium chloride, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 6 (mg/ml) | |
2 | 1 | 2 | 200 (mM) |