1E59
E.coli cofactor-dependent phosphoglycerate mutase complexed with vanadate
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 | 61.249, 112.142, 40.948 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.300 |
R-factor | 0.1552 |
R-free | 0.21340 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1e58 |
RMSD bond length | 0.013 |
RMSD bond angle | 0.029 |
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 | 1.310 |
High resolution limit [Å] | 1.300 | 1.300 |
Rmerge | 0.079 * | 0.401 * |
Number of reflections | 68073 | |
<I/σ(I)> | 17 | 2.1 |
Completeness [%] | 96.6 | 99.9 |
Redundancy | 3.1 * | 3.1 * |
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, 100 MM NAVO3 |
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) | pH8.0 |
3 | 1 | drop | 100 (mM) | ||
4 | 1 | reservoir | Tris-HCl | 100 (mM) | pH8.75 |
5 | 1 | reservoir | 200 (mM) | ||
6 | 1 | reservoir | PEG4000 | 20 (%(w/v)) | |
7 | 1 | reservoir | 100 (mM) |