3SPE
Crystal structure of the tail sheath protein protease resistant fragment from bacteriophage phiKZ
Experimental procedure
Experimental method | MAD |
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 | 2010-05-07 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97948, 0.97962, 0.94949 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 70.892, 156.715, 61.003 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.424 - 2.400 |
R-factor | 0.2579 |
Rwork | 0.256 |
R-free | 0.28650 |
Structure solution method | MAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.294 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SHELXCD |
Refinement software | PHENIX (1.7_650) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 30.000 | 30.000 | 2.490 |
High resolution limit [Å] | 2.400 | 5.160 | 2.400 |
Rmerge | 0.107 | 0.059 | 0.646 |
Number of reflections | 26951 | ||
Completeness [%] | 98.6 | 99.5 | 99.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 293 | 1.8 M Na/K Phosphate, pH 5.0 with 0.1 M Na Acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |