5C2K
Crystal structure of the fusion protein linked by RhoA and the GAP domain of MgcRacGAP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL32XU |
Synchrotron site | SPring-8 |
Beamline | BL32XU |
Temperature [K] | 110 |
Detector technology | CCD |
Collection date | 2012-10-05 |
Detector | MARRESEARCH |
Wavelength(s) | 1.00 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 44.491, 77.041, 62.253 |
Unit cell angles | 90.00, 108.53, 90.00 |
Refinement procedure
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.470 |
High resolution limit [Å] | 1.420 | 1.420 |
Number of reflections | 73586 | |
<I/σ(I)> | 21.9 | 3.4 |
Completeness [%] | 99.1 | 94.7 |
Redundancy | 4.2 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293 | PEG3350, Bis-Tris |