7RTA
Crystal structures of human PYY and NPY
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-05-02 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 62 2 2 |
| Unit cell lengths | 136.830, 136.830, 116.985 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 44.790 - 2.600 |
| R-factor | 0.2198 |
| Rwork | 0.217 |
| R-free | 0.27040 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | generic Fab |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.555 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | PHASER (2.8.2) |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 44.790 | 44.790 | 2.720 |
| High resolution limit [Å] | 2.600 | 9.010 | 2.600 |
| Rmerge | 0.144 | 0.042 | 1.451 |
| Rmeas | 0.150 | 0.044 | 1.512 |
| Rpim | 0.043 | 0.014 | 0.420 |
| Total number of observations | 249910 | 5931 | 30662 |
| Number of reflections | 20402 | 578 | 2409 |
| <I/σ(I)> | 13 | 40.6 | 2 |
| Completeness [%] | 99.9 | 99.2 | 99.5 |
| Redundancy | 12.2 | 10.3 | 12.7 |
| CC(1/2) | 0.998 | 0.999 | 0.720 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | Protein complex (~4 mg/mL with respect to Fab, NPY:Fab at molar ratio of 1.4:1, all dissolved in 25 mM Tris (pH 7.5), 100 mM NaCl) was combined to an equal volume (2 uL) of well solution comprising 200 mM Li2SO4, 100 mM sodium acetate (pH 4.5), 22% (w/v) PEG1000 |
