5TQ1
Phospholipase C gamma-1 C-terminal SH2 domain bound to a phosphopeptide derived from the insulin receptor
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.2 |
Synchrotron site | ALS |
Beamline | 8.2.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-12-10 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 34.010, 55.140, 58.665 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.332 - 1.485 |
R-factor | 0.1736 |
Rwork | 0.172 |
R-free | 0.20990 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4k44 |
RMSD bond length | 0.004 |
RMSD bond angle | 0.834 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.3.20) |
Phasing software | PHASER (2.3.0) |
Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 58.665 | 58.665 | 1.560 |
High resolution limit [Å] | 1.485 | 4.690 | 1.485 |
Rmerge | 0.041 | 0.223 | |
Rmeas | 0.064 | ||
Rpim | 0.024 | ||
Total number of observations | 104032 | ||
Number of reflections | 18758 | ||
<I/σ(I)> | 16.5 | 14.6 | 2.2 |
Completeness [%] | 99.5 | 98.7 | 97.5 |
Redundancy | 5.5 | 7.1 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 9 | 277 | 0.1M Tris (pH 9.0), 30% PEG MME 2000 |