4XI2
Crystal Structure of an auto-inhibited form of Bruton's Tryrosine Kinase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE A1 |
Synchrotron site | CHESS |
Beamline | A1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-11-02 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.9474 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 132.202, 132.202, 107.632 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 43.273 - 2.600 |
R-factor | 0.2306 |
Rwork | 0.230 |
R-free | 0.24830 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.114 |
Data reduction software | DENZO (1.97.8) |
Data scaling software | SCALEPACK (1.97.7) |
Phasing software | SHARP (1.4) |
Refinement software | PHENIX ((phenix.refine: dev_1839)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.300 | 2.660 |
High resolution limit [Å] | 2.600 | 2.600 |
Number of reflections | 30976 | |
<I/σ(I)> | 10.6 | 1.1 |
Completeness [%] | 91.9 | 69.6 |
Redundancy | 4.8 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 277 | Mix purified dimer protein at 5 mg/ml in 25 mM TRIS.Cl, pH 8.5, 10 mM NaCl, 5 mM DTT with an equal volume of the precipitant solution, 100 mM TRIS.Cl, pH 8.5, 200 mM Na.acetate, 7.5 % PEG 4,000, then suspend over 1 ml of precipitant solution. Wedge shaped crystals grew to approximately 0.1 mm on a side after a period of two weeks. Crystals were frozen by first transferring them, in four sequential steps, to a solution of 100 mM TRIS.Cl, pH 8.5, 200 mM Na.acetate, 15 % PEG 4,000. This was followed by transfer in six sequential steps to a solution containing 100 mM TRIS.Cl, pH 8.5, 200 mM Na.acetate, 15 % PEG 4,000, 30% glucose |