1AUK
HUMAN ARYLSULFATASE A
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX9.5 |
| Synchrotron site | SRS |
| Beamline | PX9.5 |
| Temperature [K] | 277 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-03 |
| Detector | MARRESEARCH |
| Spacegroup name | I 4 2 2 |
| Unit cell lengths | 132.630, 132.630, 192.060 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.100 |
| R-factor | 0.248 |
| Rwork | 0.232 |
| R-free | 0.27300 |
| Structure solution method | MIRAS |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.800 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.200 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.063 * | 0.276 * |
| Number of reflections | 49794 | |
| <I/σ(I)> | 9.4 | 4.3 |
| Completeness [%] | 96.1 | 96.7 * |
| Redundancy | 6.2 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.4 | 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, vapor diffusion - hanging drop |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | sodium acetate | 100 (mM) | |
| 2 | 1 | reservoir | PEG6000 | 10-13 (%) | |
| 3 | 1 | drop | sodium acetate | 100 (mM) | |
| 4 | 1 | drop | PEG6000 | 10-13 (%) | |
| 5 | 1 | drop | octyl-beta-glucopyranoside | 1.25 (%) | |
| 6 | 1 | drop | Tris-HCl | 10 (mM) | |
| 7 | 1 | drop | 150 (mM) |
