1SO8
Abeta-bound human ABAD structure [also known as 3-hydroxyacyl-CoA dehydrogenase type II (Type II HADH), Endoplasmic reticulum-associated amyloid beta-peptide binding protein (ERAB)]
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 32-ID |
Synchrotron site | APS |
Beamline | 32-ID |
Temperature [K] | 100 |
Spacegroup name | P 4 3 2 |
Unit cell lengths | 130.000, 130.000, 130.000 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.830 - 2.300 |
R-factor | 0.231 |
Rwork | 0.231 |
R-free | 0.26100 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 1.100 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | GLRF |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.051 | 0.152 |
Number of reflections | 17049 | |
<I/σ(I)> | 57.7 | 13 |
Completeness [%] | 99.8 | 99.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 295 | Abeta, MES, NaCl, DTT, NAD, benzamidine, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K |