1JF6
Crystal structure of thermoactinomyces vulgaris r-47 alpha-amylase mutant F286Y
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 | 2000-11-27 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 112.250, 117.940, 113.320 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.390 - 3.200 |
R-factor | 0.204 |
Rwork | 0.204 |
R-free | 0.28300 * |
RMSD bond length | 0.010 |
RMSD bond angle | 24.800 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 30.000 * |
High resolution limit [Å] | 3.200 |
Rmerge | 0.121 |
Total number of observations | 131344 * |
Number of reflections | 23309 |
<I/σ(I)> | 5.8 |
Completeness [%] | 91.7 |
Redundancy | 5.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.1 | 11 * | Kamitori, S., (1999) J.Mol.Biol., 287, 907. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG6000 | 2 (%(w/v)) | |
2 | 1 | reservoir | 2.5 (mM) | ||
3 | 1 | reservoir | MES | 20 (mM) | |
4 | 1 | drop | protein | 20 (mg/ml) |