3TJY
Structure of the Pto-binding domain of HopPmaL generated by limited chymotrypsin digestion
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-07-10 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97942 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 57.427, 57.427, 54.800 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.682 - 1.700 |
R-factor | 0.1894 |
Rwork | 0.188 |
R-free | 0.21740 |
Structure solution method | SAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.152 |
Refinement software | PHENIX ((phenix.refine: 1.7.1_743)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.682 | 1.680 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.080 | 0.501 |
Number of reflections | 11555 | |
<I/σ(I)> | 42.133 | 3.7 |
Completeness [%] | 99.9 | 100 |
Redundancy | 9.3 | 9.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 294 | 0.1M Bis-Tris pH 6.5 plus 1.5M Ammonium Sulphate. 0.03 mg/ml chymotrypsin was added to the protein prior to adding crystallization liquor. Crystals were cryoprotected with Paratone-N oil , VAPOR DIFFUSION, HANGING DROP, temperature 294K |