6AWL
Crystal structure of human Coq9
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 | PIXEL |
Collection date | 2016-02-07 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.0332 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 38.110, 97.390, 63.650 |
Unit cell angles | 90.00, 95.40, 90.00 |
Refinement procedure
Resolution | 48.690 - 2.000 |
R-factor | 0.2003 |
Rwork | 0.197 |
R-free | 0.24540 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4rhp |
RMSD bond length | 0.003 |
RMSD bond angle | 0.661 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.690 | 2.071 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.091 | 1.355 |
Rpim | 0.044 | 0.658 |
Number of reflections | 31242 | 3066 |
<I/σ(I)> | 12.38 | 1.25 |
Completeness [%] | 100.0 | 99.9 |
Redundancy | 5.1 | 5.1 |
CC(1/2) | 0.998 | 0.480 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | Protein was dissolved at 4.89 mg/mL in a buffer containing 10 mM HEPES pH 7.5, 100 mM NaCl, 0.3 mM TCEP. 200 nL of protein was mixed with 200 nL of reservoir in a SD2 plate. The reservoir consisted of 21% w/v PEG 3350, 0.25 M NaCl, and 0.1 M bistris pH 6.5. Crystals were cryopreserved in 35% PEG 3350, 0.2 M NaCl and 0.1 M bistris buffer, pH 6.5. |