5I3J
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 |
Unit cell lengths | 40.030, 44.120, 71.700 |
Unit cell angles | 79.06, 77.49, 63.11 |
Refinement procedure
Resolution | 35.300 - 1.800 |
R-factor | 0.166 |
Rwork | 0.163 |
R-free | 0.21060 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3tim |
RMSD bond length | 0.017 |
RMSD bond angle | 0.650 |
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] | 35.300 | 1.864 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.095 | |
Number of reflections | 36591 | |
<I/σ(I)> | 7.41 | |
Completeness [%] | 92.8 | |
Redundancy | 2 |
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 |