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 |
