6D87
Structure of the Bovine p85alpha BH domain, R262T mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CLSI BEAMLINE 08B1-1 |
Synchrotron site | CLSI |
Beamline | 08B1-1 |
Temperature [K] | 80 |
Detector technology | CCD |
Collection date | 2015-10-25 |
Detector | RAYONIX MX300HE |
Wavelength(s) | 0.987 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 85.499, 91.637, 93.574 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 35.795 - 2.700 |
R-factor | 0.198 |
Rwork | 0.196 |
R-free | 0.23820 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1pbw |
RMSD bond length | 0.003 |
RMSD bond angle | 0.630 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((1.13_2998)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.800 | 2.750 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.089 | 0.501 |
Number of reflections | 20681 | 1024 |
<I/σ(I)> | 23.3 | |
Completeness [%] | 99.3 | 100 |
Redundancy | 7.4 | 7.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | 1.5 M Li2SO4, 100 mM Na Cacodylate, pH 6.0 |