6JL9
Crystal structure of a frog ependymin related protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 7A (6B, 6C1) |
Synchrotron site | PAL/PLS |
Beamline | 7A (6B, 6C1) |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2018-07-25 |
Detector | ADSC QUANTUM 270 |
Wavelength(s) | 1.540 |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 61.208, 61.208, 236.196 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 53.010 - 2.000 |
R-factor | 0.19819 |
Rwork | 0.194 |
R-free | 0.27753 |
Structure solution method | SAD |
RMSD bond length | 0.014 |
RMSD bond angle | 1.740 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 53.010 | 2.030 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 18642 | |
<I/σ(I)> | 70.5 | |
Completeness [%] | 99.7 | |
Redundancy | 19.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 298 | 0.2M Calcium acetate hydrate, 0.1M Sodium cacodylate trihydrate pH 6.5, 18%(w/v) Polyethylene glycol 8,000 |