3C9Q
Crystal structure of the uncharacterized human protein C8orf32 with bound peptide
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 | 2008-02-06 |
Detector | MARMOSAIC 300 mm CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 34.322, 64.039, 113.660 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 32.857 - 1.500 |
R-factor | 0.162 |
Rwork | 0.161 |
R-free | 0.18000 |
Structure solution method | SAD |
RMSD bond length | 0.016 |
RMSD bond angle | 1.545 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHARP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 32.857 | 32.857 | 1.530 |
High resolution limit [Å] | 1.498 | 3.700 | 1.498 |
Rmerge | 0.105 | 0.058 | 0.543 |
Number of reflections | 40943 | ||
<I/σ(I)> | 12.075 | 2.526 | |
Completeness [%] | 99.5 | 99.5 | 95.9 |
Redundancy | 12.2 | 12.6 | 6.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 291 | Protein solution (10 mg/mL Se-Met protein, 0.050 M Sodium chloride, 0.003 M Sodium azide, 0.0003 M TCEP, Bis-Tris pH 7.0) mixed in a 1:1 ratio with the Well solution (1% Ethylene glycol, 1.8 M Ammonium sulfate, 0.10 M MES pH 6.0). Cryoprotected in four stages with well solution using 0 to 25 % ethylene glycol, VAPOR DIFFUSION, HANGING DROP, temperature 291K |