5CF3
Crystal structures of Bbp from Staphylococcus aureus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U |
Synchrotron site | SSRF |
Beamline | BL17U |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-08-23 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.979 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 96.241, 98.924, 102.257 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.593 - 2.031 |
R-factor | 0.2185 |
Rwork | 0.217 |
R-free | 0.25350 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4f24 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.097 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.100 |
High resolution limit [Å] | 2.030 | 4.370 | 2.030 |
Rmerge | 0.078 | 0.042 | 0.448 |
Total number of observations | 115200 | ||
Number of reflections | 31074 | ||
<I/σ(I)> | 12 | ||
Completeness [%] | 96.8 | 95.9 | 89.3 |
Redundancy | 3.7 | 3.7 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 291.15 | crystals were grown in 0.2 M calcium acetate hydrate, 0.1 M sodium cacodylate trihydrate pH6.5, 18% PEG8000 Protein concentration was 30mg/ml |