3CT1
Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 14-BM-C |
Synchrotron site | APS |
Beamline | 14-BM-C |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 30.800, 69.388, 71.208 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 35.600 - 1.510 |
R-factor | 0.19357 |
Rwork | 0.192 |
R-free | 0.22177 |
Structure solution method | FOURIER SYNTHESIS |
RMSD bond length | 0.016 |
RMSD bond angle | 1.527 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.600 | 1.550 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.060 | 0.373 |
Number of reflections | 23681 | |
<I/σ(I)> | 24.5 | 4.4 |
Completeness [%] | 96.4 | 99.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 20% PEG4000, 100mM Tris-HCl, 10% glycerol, 10mM NAG5, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |