3KTA
Structural Basis for Adenylate Kinase Activity in ABC ATPases
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-06-26 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.933 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 65.000, 86.100, 70.100 |
Unit cell angles | 90.00, 116.60, 90.00 |
Refinement procedure
Resolution | 35.435 - 1.627 |
R-factor | 0.1775 |
Rwork | 0.176 |
R-free | 0.20620 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.138 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | CNS |
Refinement software | PHENIX (1.5_2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.645 |
High resolution limit [Å] | 1.600 | 1.600 |
Number of reflections | 84052 | |
Completeness [%] | 95.7 | 95.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.6 | 298 | BisTRIS, 16% PEG3350, pH 6.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K |