3N94
Crystal structure of human pituitary adenylate cyclase 1 Receptor-short N-terminal extracellular domain
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 | 2010-03-12 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.978 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.987, 92.151, 105.418 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 69.380 - 1.800 |
| R-factor | 0.178 |
| Rwork | 0.176 |
| R-free | 0.21600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3c4m |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.732 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 69.380 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.090 | 0.968 |
| Number of reflections | 42645 | |
| <I/σ(I)> | 28.8 | 2.04 |
| Completeness [%] | 99.9 | 99.8 |
| Redundancy | 13.6 | 10.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293.15 | 25.5% PEG 4000, 15% Glycerol, 170mM Ammonium sulphate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293.15K |
