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 |