5HM7
The Intracellular domain of Butyrophilin 3A1 protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-06-17 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.033 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 37.430, 145.840, 44.910 |
Unit cell angles | 90.00, 105.57, 90.00 |
Refinement procedure
Resolution | 72.920 - 1.930 |
R-factor | 0.198 |
Rwork | 0.197 |
R-free | 0.22700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4n7i |
RMSD bond length | 0.011 |
RMSD bond angle | 1.491 |
Data reduction software | iMOSFLM |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0131) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 72.920 | 2.020 |
High resolution limit [Å] | 1.930 | 1.930 |
Number of reflections | 34081 | |
<I/σ(I)> | 5.63 | 1.52 |
Completeness [%] | 98.7 | 99.7 |
Redundancy | 17.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 298 | 22% PEG 3350, 0.2M Magnesium chloride, 0.1M HEPES 7.0 |