1HCU
alpha-1,2-mannosidase from Trichoderma reesei
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-01-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 86.201, 106.836, 101.388 |
| Unit cell angles | 90.00, 99.42, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.370 |
| R-factor | 0.1772 |
| Rwork | 0.177 |
| R-free | 0.23230 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1dl2 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.500 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.450 |
| High resolution limit [Å] | 2.370 | 2.370 |
| Rmerge | 0.083 | 0.214 |
| Total number of observations | 818429 * | |
| Number of reflections | 73996 | |
| <I/σ(I)> | 20.01 | 4.915 |
| Completeness [%] | 98.9 | 95.1 |
| Redundancy | 4.94 | 4.14 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.4 * | 10MG/ML PROTEIN IN 0.1M TRIS-CL PH 7.5 MIX 2 MICROLITER OF PROTEIN SOLUTION WITH 2 MICROLITER OF WELL SOLUTION IN A HANGING DROP EXPERIMENT. THE WELL CONTAINS 0.1M NA-ACETATE PH 4.0, 12% PEG 35000, 0.3M CACL2 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 20 (mM) | |
| 3 | 1 | drop | 25 (mM) | ||
| 4 | 1 | reservoir | sodium acetate | 0.1 (M) | |
| 5 | 1 | reservoir | 0.3 (M) | ||
| 6 | 1 | reservoir | PEG35000 | 12.5 (%(w/v)) |
