1MFU
Probing the role of a mobile loop in human salivary amylase: Structural studies on the loop-deleted mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE F1 |
| Synchrotron site | CHESS |
| Beamline | F1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-03-31 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.91 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 52.074, 73.815, 135.787 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 26.540 - 2.000 |
| R-factor | 0.16226 |
| Rwork | 0.160 |
| R-free | 0.20109 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1jxk |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.368 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 26.540 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.060 | 0.267 |
| Number of reflections | 35031 | |
| <I/σ(I)> | 24.5 | 7 |
| Completeness [%] | 96.8 | |
| Redundancy | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | soaking with acarbose at 1 mM concentration for 24 hours | 9 | 298 | 40% mpd, pH 9.0, soaking with acarbose at 1 mM concentration for 24 hours, temperature 298K |
