5I3I
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 | 2012-08-06 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.284 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 69.730, 87.500, 76.300 |
| Unit cell angles | 90.00, 107.27, 90.00 |
Refinement procedure
| Resolution | 58.570 - 2.200 |
| R-factor | 0.2053 |
| Rwork | 0.203 |
| R-free | 0.24940 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3tim |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.575 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 58.570 | 2.279 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.058 | |
| Number of reflections | 42618 | |
| <I/σ(I)> | 7.53 | |
| Completeness [%] | 95.7 | |
| Redundancy | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 287 | 20-30% MePEG 5000, 2-4% PEP, 50 mM MES |
