1C4R
THE STRUCTURE OF THE LIGAND-BINDING DOMAIN OF NEUREXIN 1BETA: REGULATION OF LNS DOMAIN FUNCTION BY ALTERNATIVE SPLICING
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL1-5 |
| Synchrotron site | SSRL |
| Beamline | BL1-5 |
| Temperature [K] | 110 |
| Wavelength(s) | 1.0712, 0.9791, 0.9793, 0.9221 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 116.600, 195.900, 103.610 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.600 |
| R-factor | 0.249 |
| Rwork | 0.249 |
| R-free | 0.27900 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 27.600 * |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 * | |
| High resolution limit [Å] | 2.600 * | 2.600 * |
| Rmerge | 0.095 * | 0.495 * |
| Total number of observations | 351083 * | |
| Number of reflections | 73128 * | |
| Completeness [%] | 98.1 * | 82.7 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 7.5 * | 21 * | pH 6.50 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | HEPES | 20 (mM) | |
| 3 | 1 | drop | 150 (mM) | ||
| 4 | 1 | drop | EDTA | 1 (mM) | |
| 5 | 1 | drop | 1,2,3-heptanetriol | 15 (%) | |
| 6 | 1 | reservoir | mPEG5000 | 21 (%(w/v)) | |
| 7 | 1 | reservoir | sodium cacodylate | 100 (mM) | |
| 8 | 1 | reservoir | ammonium sulfate | 200 (mM) |
