1HL8
CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-03-03 |
Detector | ADSC CCD |
Spacegroup name | H 3 2 |
Unit cell lengths | 172.462, 172.462, 167.414 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 37.000 * - 2.400 |
R-factor | 0.188 |
Rwork | 0.185 |
R-free | 0.22840 * |
Structure solution method | MAD |
RMSD bond length | 0.008 |
RMSD bond angle | 1.100 * |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | SOLVE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 37.000 * | 2.460 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.069 | 0.416 |
Total number of observations | 212598 * | |
Number of reflections | 36833 | |
<I/σ(I)> | 8.9 | 1.8 |
Completeness [%] | 99.3 * | 99.3 * |
Redundancy | 5.7 | 5.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8 | 20 * | 18 % PEG600, 5 % JEFFAMINE, M-600 100 MM TRIS-HCL PH 8.0, PROTEIN CONC. 5 MG/ML |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5.0 (mg/ml) | |
2 | 1 | reservoir | PEG6000 | 18 (%(w/v)) | |
3 | 1 | reservoir | Tris-HCl | 100 (mM) | pH8.0 |
4 | 1 | reservoir | Jeffamine M-600 | 5 (%) |