3LMG
Crystal structure of the ERBB3 kinase domain in complex with AMP-PNP
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 | 2009-03-13 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97949 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 193.348, 47.981, 82.224 |
| Unit cell angles | 90.00, 108.11, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.800 |
| R-factor | 0.255 |
| Rwork | 0.252 |
| R-free | 0.28500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2gs7 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.099 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.850 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.114 | 0.499 |
| Number of reflections | 16021 | |
| <I/σ(I)> | 8.8 | 2.2 |
| Completeness [%] | 90.0 | 55.3 |
| Redundancy | 6.3 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 294 | 50 mM MOPS pH7.4, 27% (w/v) PEG8000, 0.17 M ammonium sulfate and 15%(v/v) glycerol in well solution and 5mM MgCl2 and 1mM AMP-PNP in protein solution, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
