1EPF
CRYSTAL STRUCTURE OF THE TWO N-TERMINAL IMMUNOGLOBULIN DOMAINS OF THE NEURAL CELL ADHESION MOLECULE (NCAM)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 120 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-08-28 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 47.078, 122.505, 72.859 |
| Unit cell angles | 90.00, 98.27, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.850 |
| R-factor | 0.201 |
| Rwork | 0.201 |
| R-free | 0.23400 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 27.500 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.920 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.047 | 0.308 |
| Total number of observations | 186351 * | |
| Number of reflections | 64828 | |
| <I/σ(I)> | 21.9 | |
| Completeness [%] | 92.6 | 90 |
| Redundancy | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 * | 293 * | used macroseeding, Kasper, C., (1999) Acta Crystallogr., Sect.D, 55, 1598. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 3.5 (mg/ml) | |
| 2 | 1 | drop | HEPES | 10 (mM) | |
| 3 | 1 | drop | 15 (mM) | ||
| 4 | 1 | reservoir | PEG4000 | 12-13 (%) | |
| 5 | 1 | reservoir | 15 (mM) |
