5FBM
Crystal Structure of Histone Like Protein (HLP) from Streptococcus mutans Refined to 1.9 A Resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-12-07 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 32.458, 76.333, 36.933 |
| Unit cell angles | 90.00, 107.21, 90.00 |
Refinement procedure
| Resolution | 38.166 - 1.900 |
| R-factor | 0.1785 |
| Rwork | 0.177 |
| R-free | 0.21670 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3rhi |
| RMSD bond length | 0.010 |
| RMSD bond angle | 0.962 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.2.14) |
| Phasing software | PHASER (2.5.5) |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 38.170 | 38.170 | 1.940 |
| High resolution limit [Å] | 1.900 | 9.110 | 1.900 |
| Rmerge | 0.051 | 0.026 | 0.714 |
| Rpim | 0.033 | 0.017 | 0.454 |
| Total number of observations | 45407 | 391 | 2971 |
| Number of reflections | 13437 | ||
| <I/σ(I)> | 13.8 | 40.1 | 1.9 |
| Completeness [%] | 98.8 | 87 | 99.4 |
| Redundancy | 3.4 | 3.3 | 3.4 |
| CC(1/2) | 0.999 | 0.998 | 0.710 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 10.5 | 293 | 30% PEG 400 and 0.1M CAPS |






