5I3K
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 | SYNCHROTRON |
Source details | SSRL BEAMLINE BL7-1 |
Synchrotron site | SSRL |
Beamline | BL7-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-05-21 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.284 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 69.890, 87.600, 76.380 |
Unit cell angles | 90.00, 107.35, 90.00 |
Refinement procedure
Resolution | 72.910 - 2.209 |
R-factor | 0.2213 |
Rwork | 0.219 |
R-free | 0.26440 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3tim |
RMSD bond length | 0.003 |
RMSD bond angle | 0.431 |
Data reduction software | HKL-2000 |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 72.910 | 2.288 |
High resolution limit [Å] | 2.209 | 2.209 |
Rmerge | 0.062 | |
Number of reflections | 43105 | |
<I/σ(I)> | 7.45 | |
Completeness [%] | 97.5 | |
Redundancy | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 287 | 20-30% Peg 4000, 150-250 mM NaCl, 50 mM Epps |