4O0M
Crystal structure of T. Elongatus BP-1 Clock Protein KaiC
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-11-28 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97856 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 130.810, 195.290, 136.640 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 58.995 - 2.840 |
R-factor | 0.2271 |
Rwork | 0.225 |
R-free | 0.26960 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 0.807 |
Data reduction software | HKL-2000 |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.8.2_1309)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 59.000 | 2.900 |
High resolution limit [Å] | 2.840 | 2.840 |
Rmerge | 0.110 | 0.769 |
Number of reflections | 79142 | |
<I/σ(I)> | 9.6 | 1.8 |
Completeness [%] | 99.1 | 99.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 4.5 | 291 | Acetate buffer and 1M sodium formate, pH 4.5, VAPOR DIFFUSION, temperature 291K |