1XGZ
Structure of the N298S variant of human pancreatic alpha-amylase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 298 |
| Detector technology | IMAGE PLATE |
| Collection date | 2002-08-16 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 52.910, 68.900, 131.770 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.000 |
| Rwork | 0.155 |
| R-free | 0.20000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1bsi |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.600 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 25.000 |
| High resolution limit [Å] | 2.000 |
| Rmerge | 0.055 |
| Number of reflections | 33697 |
| Completeness [%] | 93.0 |
| Redundancy | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | MPD, cacodylate, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
