1URH
The "Rhodanese" fold and catalytic mechanism of 3-mercaptopyruvate sulfotransferases: Crystal structure of SseA from Escherichia coli
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Collection date | 2002-07-15 |
| Spacegroup name | P 43 |
| Unit cell lengths | 150.170, 150.170, 37.930 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 2.800 |
| R-factor | 0.234 |
| Rwork | 0.234 |
| R-free | 0.28900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1rhs |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.400 |
| 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] | 40.000 | 2.850 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.066 | 0.483 |
| Total number of observations | 312079 * | |
| Number of reflections | 21524 | |
| <I/σ(I)> | 16 | 2 |
| Completeness [%] | 95.6 * | 97.9 |
| Redundancy | 14 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 * | 294 * | Spallarossa, A., (2003) Acta Cryst., D59, 168. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 14 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 50 (mM) | pH8.0 |
| 3 | 1 | drop | 50 (mM) | ||
| 4 | 1 | reservoir | ammonium sulfate | 1.9 (M) | |
| 5 | 1 | reservoir | MES | 40 (mM) | pH6.2 |
| 6 | 1 | reservoir | PEG400 | 2 (%(v/v)) | |
| 7 | 1 | reservoir | 10 (mM) |
