5KSO
hMiro1 C-domain GDP-Pi Complex P3121 Crystal Form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-08-08 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.978590 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 65.510, 65.510, 82.520 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 33.369 - 2.250 |
R-factor | 0.1785 |
Rwork | 0.175 |
R-free | 0.20900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4c0l |
RMSD bond length | 0.003 |
RMSD bond angle | 0.680 |
Data reduction software | MOSFLM (7.1.0) |
Data scaling software | Aimless (0.3.8) |
Phasing software | PHENIX (2.5.6) |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 82.500 | |
High resolution limit [Å] | 2.250 | 2.250 |
Rmerge | 0.083 | |
Number of reflections | 10140 | |
<I/σ(I)> | 83 | |
Completeness [%] | 100.0 | |
Redundancy | 20 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5 | 294 | 19 mg/mL protein, 5 mM magnesium chloride, 0.1 M SPG buffer, pH 5.0, 25% w/v PEG1500, GDP observed in the structure was carried through from the expression system during purification |