5CFA
Crystal structures of Bbp from Staphylococcus aureus with peptide ligand
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 | 2014-06-28 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 60.916, 74.961, 75.563 |
| Unit cell angles | 90.00, 102.91, 90.00 |
Refinement procedure
| Resolution | 36.560 - 1.450 |
| R-factor | 0.18 |
| Rwork | 0.178 |
| R-free | 0.21220 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5cf3 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.140 |
| 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 | 1.500 |
| High resolution limit [Å] | 1.450 | 3.120 | 1.450 |
| Rmerge | 0.084 | 0.051 | 0.865 |
| Rmeas | 0.093 | 0.057 | 0.976 |
| Rpim | 0.041 | 0.025 | 0.442 |
| Total number of observations | 591166 | ||
| Number of reflections | 116230 | ||
| <I/σ(I)> | 6.9 | ||
| Completeness [%] | 99.2 | 99.6 | 95.8 |
| Redundancy | 5.1 | 5.3 | 4.5 |
| CC(1/2) | 0.997 | 0.747 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291.15 | peptide was added into the concentrated protein samples at 10:1 ratio and the protein-peptide complex crystals are grown in 0.2 M lithium sulfate, 0.1M Tris-HCl pH8.2, 30% PEG4000 protein concentration was 30mg/ml |
