3O69
Structure of the E100A E.coli GDP-mannose hydrolase (yffh) in complex with Mg++
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E DW |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-08-18 |
| Detector | RIGAKU SATURN 944+ |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 60.379, 69.260, 98.554 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 22.810 - 2.100 |
| R-factor | 0.2084 |
| Rwork | 0.205 |
| R-free | 0.27960 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3o52 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.262 |
| 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] | 22.810 | 50.000 | 2.180 |
| High resolution limit [Å] | 2.100 | 4.520 | 2.100 |
| Rmerge | 0.089 | 0.049 | 0.331 |
| Number of reflections | 23871 | ||
| <I/σ(I)> | 12.8 | ||
| Completeness [%] | 96.0 | 98.4 | 75.1 |
| Redundancy | 5.6 | 5.8 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 291 | 20-26% PEG 3350, 0.2 M Mg Cl, 0.1 M Tris HCL pH 8.5, 4mM GDP-mannose at a ratio of 1:1 protein:reservoir, vapor diffusion, hanging drop, temperature 291K |
