4X57
Structure of an Arabidopsis E2 / Membrane-anchored Ubiquitin-fold Protein Complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-04-20 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 0.97934 |
| Spacegroup name | P 63 2 2 |
| Unit cell lengths | 135.716, 135.716, 202.134 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 10.000 - 2.800 |
| R-factor | 0.22301 |
| Rwork | 0.221 |
| R-free | 0.25682 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | ID 3NOB 1qcq |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.544 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.850 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.070 | 1.000 |
| Number of reflections | 27721 | |
| <I/σ(I)> | 30 | 1.95 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 7.2 | 7.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 280 | 3.0 M (NH4)2SO4 |
