3BQW
Crystal structure of the putative capsid protein of prophage (E.coli CFT073)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-BM |
Synchrotron site | APS |
Beamline | 19-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-10-29 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9794 |
Spacegroup name | P 61 |
Unit cell lengths | 113.624, 113.624, 58.863 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 98.530 - 2.200 |
R-factor | 0.17732 |
Rwork | 0.175 |
R-free | 0.22510 |
Structure solution method | SAD |
RMSD bond length | 0.014 |
RMSD bond angle | 1.419 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 98.530 | 2.256 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.140 | 0.527 |
Number of reflections | 20956 | |
<I/σ(I)> | 18.39 | 2.47 |
Completeness [%] | 99.4 | 98.28 |
Redundancy | 10.6 | 7.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.2 | 289 | 10% PEG 3000, 0.1M Na/K phosphate, pH 6.2, VAPOR DIFFUSION, SITTING DROP, temperature 289K |