1E33
Crystal structure of an Arylsulfatase A mutant P426L
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] | 277 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-12-15 |
| Detector | MARRESEARCH |
| Spacegroup name | I 4 2 2 |
| Unit cell lengths | 131.400, 131.400, 192.000 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.500 |
| R-factor | 0.187 |
| Rwork | 0.185 |
| R-free | 0.25000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1auk |
| RMSD bond length | 0.020 |
| RMSD bond angle | 0.053 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.600 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.083 * | 0.360 * |
| Total number of observations | 151131 * | |
| Number of reflections | 29188 | |
| <I/σ(I)> | 14.9 | 2.8 |
| Completeness [%] | 99.2 | 99.3 |
| Redundancy | 5.4 | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.4 * | 18 * | PROTEIN WAS CRYSTALLIZED BY VAPOR DIFFUSION IN HANGING DROPS AT 291 K. SOLUTION CONTAINING 10MG/ML PROTEIN, 10 MM TRIS/HCL (PH 7.4) AND 150 MM NACL WAS MIXED WITH SAME VOLUME OF RESERVOIR SOLUTION, CONTAINING 100 MM NA-ACETATE (PH 5.0 - 5.4) AND 10 - 13 % PEG 6000 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | drop | 150 (mM) | ||
| 4 | 1 | reservoir | sodium acetate | 100 (mM) | |
| 5 | 1 | reservoir | PEG6000 | 10-13 (%) |
