3CSQ
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 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-06-21 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.03 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 53.842, 133.963, 85.725 |
Unit cell angles | 90.00, 89.99, 90.00 |
Refinement procedure
Resolution | 19.900 - 1.800 |
R-factor | 0.24046 |
Rwork | 0.238 |
R-free | 0.28239 |
Structure solution method | SIR+SAD |
RMSD bond length | 0.014 |
RMSD bond angle | 1.565 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SHELX (& SHARP) |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.900 | 1.850 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.055 | 0.109 |
Number of reflections | 109340 | |
<I/σ(I)> | 20 | 9.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 100mM Tris-HCl, 200mM MgCl2, 28% (w/v) PEG4000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |