1HX0
Structure of pig pancreatic alpha-amylase complexed with the "truncate" acarbose molecule (pseudotrisaccharide)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-11-20 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.933 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 69.280, 113.550, 117.160 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 35.000 - 1.380 |
R-factor | 0.1083 |
Rwork | 0.108 |
R-free | 0.13020 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ppi |
RMSD bond length | 0.013 * |
RMSD bond angle | 0.030 * |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.000 | 1.420 |
High resolution limit [Å] | 1.380 | 1.380 |
Rmerge | 0.067 | 0.451 * |
Total number of observations | 507677 * | |
Number of reflections | 184003 | |
<I/σ(I)> | 13.1 | 1.93 |
Completeness [%] | 97.0 | 96.13 |
Redundancy | 2.8 | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | batch | 8.5 | 277 | Qian, M., (1993) J. Mol. Biol., 232, 785. * |