1E58
E.coli cofactor-dependent phosphoglycerate mutase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX9.6 |
| Synchrotron site | SRS |
| Beamline | PX9.6 |
| Temperature [K] | 105 |
| Collection date | 1999-09-15 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 61.570, 113.000, 40.260 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.250 |
| R-factor | 0.121 |
| R-free | 0.16800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.014 |
| RMSD bond angle | 0.030 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHELX |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.260 |
| High resolution limit [Å] | 1.250 | 1.250 |
| Rmerge | 0.047 * | 0.071 * |
| Number of reflections | 67122 | |
| <I/σ(I)> | 211 | 11 |
| Completeness [%] | 85.4 | 63 |
| Redundancy | 2 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 * | 100 MM TRIS-HCL (PH 8.0), 200 MM LI2SO4, 20% PEG 4000 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 15 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 20 (mM) | |
| 3 | 1 | drop | 100 (mM) | ||
| 4 | 1 | reservoir | Tris-HCl | 100 (mM) | |
| 5 | 1 | reservoir | 200 (mM) | ||
| 6 | 1 | reservoir | PEG4000 | 20 (%) |
