2WHE
Structure of native Beta-Phosphoglucomutase in an open conformation without bound ligands.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-09-28 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 53.239, 56.900, 75.441 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.550 |
| R-factor | 0.177 |
| Rwork | 0.176 |
| R-free | 0.20800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1zol |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.686 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0070) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.500 | 1.630 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.060 | 0.340 |
| Number of reflections | 28532 | |
| <I/σ(I)> | 10.7 | 2.1 |
| Completeness [%] | 84.3 | 43.1 |
| Redundancy | 2.4 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.2 | 28-29 % PEG 4000 AND 200 MM NA ACETATE, pH 7.2 |
