2IPM
Crystal structure of a disulfide mutant glucose binding protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.1 |
Synchrotron site | ALS |
Beamline | 8.2.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-06-06 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 61.190, 36.600, 64.820 |
Unit cell angles | 90.00, 106.81, 90.00 |
Refinement procedure
Resolution | 31.430 - 1.120 |
R-factor | 0.159 |
Rwork | 0.158 |
R-free | 0.17900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2hph |
RMSD bond length | 0.007 |
RMSD bond angle | 1.285 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.190 |
High resolution limit [Å] | 1.120 | 1.120 |
Rmerge | 0.063 | 0.263 |
Number of reflections | 103523 | |
<I/σ(I)> | 11.2 | 3.5 |
Completeness [%] | 100.0 | 99.2 |
Redundancy | 3.2 | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 290 | 20% PEG 6000, 50mM HEPES, pH7.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K |