1JI1
Crystal Structure Analysis of Thermoactinomyces vulgaris R-47 alpha-Amylase 1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-6A |
Synchrotron site | Photon Factory |
Beamline | BL-6A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-11-26 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 122.570, 50.840, 107.800 |
Unit cell angles | 90.00, 104.20, 90.00 |
Refinement procedure
Resolution | 20.000 * - 1.600 |
R-factor | 0.182 * |
Rwork | 0.182 |
R-free | 0.20600 |
Structure solution method | MIR |
RMSD bond length | 0.005 |
RMSD bond angle | 24.800 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | MLPHARE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 * | |
High resolution limit [Å] | 1.600 | 1.600 * |
Rmerge | 0.061 | 0.219 * |
Total number of observations | 391238 * | |
Number of reflections | 152851 | |
Completeness [%] | 89.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | Kondo, S., (2000) Protein Pept. Letters, 7, 197., Kamitori, S., (1995) J. Struct. Biol., 114, 229. * |