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 |