1Q4N
Structural studies of Phe256Trp of human salivary alpha-amylase: implications for the role of a conserved water molecule and its associated chain in enzyme activity
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2001-12-01 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 51.900, 74.200, 134.820 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 * - 2.100* |
| R-factor | 0.15874 |
| Rwork | 0.156 |
| R-free | 0.20400 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1mfv |
| RMSD bond length | 0.017 * |
| RMSD bond angle | 1.500 * |
| 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] | 20.000 * | 2.140 |
| High resolution limit [Å] | 2.100 * | 2.070 |
| Rmerge | 0.060 | |
| Total number of observations | 89732 * | |
| Number of reflections | 30610 | |
| <I/σ(I)> | 13 | |
| Completeness [%] | 94.5 | 60 |
| Redundancy | 3.0 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 9 | Ramasubbu, N., (1991) Proteins, 11, 230. * |
