1UUJ
N-terminal domain of Lissencephaly-1 protein (Lis-1)
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-08-22 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.979392,0.979528, 0.964216 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 62.988, 111.753, 47.397 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 1.750 |
| R-factor | 0.192 |
| Rwork | 0.190 |
| R-free | 0.24600 |
| Structure solution method | MAD |
| RMSD bond length | 0.017 |
| RMSD bond angle | 2.883 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | SOLVE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.810 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.057 | 0.477 |
| Number of reflections | 33378 | |
| <I/σ(I)> | 40 | 3 |
| Completeness [%] | 96.1 | 78.9 |
| Redundancy | 12 | 9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 4.5 | CRYSTALS WERE GROWN USING SITTING-DROP VAPOUR-DIFFUSION UNDER MINERAL OIL USING A 1:1 MIXTURE OF PROTEIN AND 1.7 M (NH4)2SO4 AND 0.1 M NA3-CITRATE, PH 4.5 |
