1R7L
2.0 A Crystal Structure of a Phage Protein from Bacillus cereus ATCC 14579
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-10-20 |
Detector | SBC-2 |
Wavelength(s) | 0.9795, 0.9798, 0.9465 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 37.002, 66.338, 53.966 |
Unit cell angles | 90.00, 95.29, 90.00 |
Refinement procedure
Resolution | 24.900 - 2.000 |
R-factor | 0.223 |
Rwork | 0.223 |
R-free | 0.26400 |
Structure solution method | MAD |
RMSD bond length | 0.008 |
RMSD bond angle | 1.300 |
Data scaling software | HKL-2000 |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.098 | 0.518 |
Number of reflections | 17557 | |
<I/σ(I)> | 22.3 | 2.25 |
Completeness [%] | 99.1 | 95.6 |
Redundancy | 8.12 | 7.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6 | 298 | 20% PEG 8000, 0.1M MES, 0.2M Ca(OAc)2, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K |