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. * |