1YIG
Crystal Structure of the Human EB1 C-terminal Dimerization Domain
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.3.1 |
Synchrotron site | ALS |
Beamline | 8.3.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-09-06 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.97964, 0.97979, 1.12713 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 32.981, 37.335, 56.776 |
Unit cell angles | 90.00, 106.06, 90.00 |
Refinement procedure
Resolution | 31.700 - 2.000 |
R-factor | 0.222 |
Rwork | 0.219 |
R-free | 0.25100 |
Structure solution method | MAD |
RMSD bond length | 0.006 |
RMSD bond angle | 0.900 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 31.700 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.027 | 0.110 |
Number of reflections | 14472 | |
<I/σ(I)> | 25.4 | 6.1 |
Completeness [%] | 100.0 | 40.4 |
Redundancy | 2.5 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 293 | protein stock = EB1 C-terminal domain @15 mg/ml, well = 22%, PEG 200 (v/v), 100 mM ammonium acetate pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |