3O52
Structure of the E.coli GDP-mannose hydrolase (yffh) in complex with tartrate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X6A |
| Synchrotron site | NSLS |
| Beamline | X6A |
| Temperature [K] | 100 |
| Detector technology | CCD detector |
| Collection date | 2009-04-29 |
| Detector | ACSD Q210 |
| Wavelength(s) | 0.9809 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 75.337, 103.218, 254.536 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.730 - 2.500 |
| R-factor | 0.2151 |
| Rwork | 0.211 |
| R-free | 0.28850 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1viu |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.456 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 29.730 | 30.000 | 2.540 |
| High resolution limit [Å] | 2.500 | 6.760 | 2.500 |
| Rmerge | 0.069 | 0.044 | 0.344 |
| Number of reflections | 33433 | ||
| <I/σ(I)> | 13.4 | ||
| Completeness [%] | 96.4 | 96.9 | 80.7 |
| Redundancy | 7.2 | 6.5 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 291 | 1.5 M KNa Tartrate, 0.1 M Bis Tris propane pH 7.5 at a ratio of 2:1 protein:reservoir, vapor diffusion, hanging drop, temperature 291K |
