6VRI
Crystal Structure of the wtBlc-split Protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2018-12-16 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 68.416, 68.416, 217.748 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 59.250 - 1.940 |
| R-factor | 0.2139 |
| Rwork | 0.212 |
| R-free | 0.24940 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1qwd |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.705 |
| Data reduction software | xia2 |
| Data scaling software | xia2 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0257) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 59.250 | 1.970 |
| High resolution limit [Å] | 1.940 | 1.940 |
| Rmeas | 0.150 | 1.627 |
| Rpim | 0.051 | 0.534 |
| Total number of observations | 403082 | |
| Number of reflections | 44856 | 1915 |
| <I/σ(I)> | 8.1 | 2.1 |
| Completeness [%] | 99.5 | 86.2 |
| Redundancy | 9 | 8.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 294 | 1.6 M ammonium sulfate, 0.1 M MES, pH 4.5, supplemented with 5% w/v n-Dodecyl-b-D-maltoside |
