5HI8
Structure of T-type Phycobiliprotein Lyase CpeT from Prochlorococcus phage P-HM1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-06-15 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 1.00005 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 63.290, 61.680, 93.340 |
| Unit cell angles | 90.00, 109.77, 90.00 |
Refinement procedure
| Resolution | 43.918 - 1.800 |
| R-factor | 0.2082 |
| Rwork | 0.207 |
| R-free | 0.22830 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4o4o |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.088 |
| Data scaling software | XSCALE (November 3, 2014) |
| Phasing software | PHASER (2.5.6) |
| Refinement software | PHENIX (1-9-1692) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.850 | |
| High resolution limit [Å] | 1.800 | 8.050 | 1.800 |
| Rmerge | 0.084 | 0.071 | 0.954 |
| Number of reflections | 60405 | ||
| <I/σ(I)> | 7.37 | 16.58 | 1.18 |
| Completeness [%] | 97.9 | 99.4 | 95.7 |
| Redundancy | 3.53 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 9.5 | 291 | 0.1 M Glycine, 0.05 M MgAcetate, 32 % PEG 400, pH 9.5 |
