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 |
