5I3G
Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-06-04 |
Detector | RIGAKU SATURN 944+ |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 |
Unit cell lengths | 46.420, 75.416, 75.779 |
Unit cell angles | 102.04, 104.78, 97.84 |
Refinement procedure
Resolution | 29.030 - 1.960 |
R-factor | 0.1749 |
Rwork | 0.172 |
R-free | 0.22160 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3tim |
RMSD bond length | 0.008 |
RMSD bond angle | 0.835 |
Data reduction software | d*TREK |
Data scaling software | d*TREK |
Phasing software | MOLREP |
Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.030 | 2.030 |
High resolution limit [Å] | 1.960 | 1.960 |
Rmerge | 0.097 | |
Number of reflections | 67582 | |
<I/σ(I)> | 7 | |
Completeness [%] | 98.9 | |
Redundancy | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 287 | 15-25% Peg 8000, 50-100 mM potassium acetate, 100 mM BTP pH 7.0 |