3RE4
Crystal Structure of Archaeoglobus Fulgidus Rio1 Kinase bound to Toyocamycin.
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] | 100 |
Detector technology | CCD |
Collection date | 2009-03-10 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97919 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 52.814, 72.607, 60.561 |
Unit cell angles | 90.00, 90.17, 90.00 |
Refinement procedure
Resolution | 34.943 - 1.997 |
R-factor | 0.2173 |
Rwork | 0.215 |
R-free | 0.25960 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.011 |
RMSD bond angle | 1.385 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | PHENIX ((phenix.refine: 1.7_650)) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 34.943 |
High resolution limit [Å] | 1.997 |
Number of reflections | 30275 |
<I/σ(I)> | 5.5 |
Completeness [%] | 97.1 |
Redundancy | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 24% PEG 3350, 0.2 M Mg (CH3COO)2, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |