1F0M
MONOMERIC STRUCTURE OF THE HUMAN EPHB2 SAM (STERILE ALPHA MOTIF) DOMAIN
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12C |
Synchrotron site | NSLS |
Beamline | X12C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1998-09-08 |
Detector | OTHER |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 54.837, 54.837, 65.545 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.200 |
R-factor | 0.243 |
Rwork | 0.243 |
R-free | 0.26400 |
RMSD bond length | 0.013 |
RMSD bond angle | 2.097 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 500.000 | 50.000 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.048 | 0.302 * |
Number of reflections | 4963 | |
<I/σ(I)> | 31 | |
Completeness [%] | 92.0 | 91.1 |
Redundancy | 8.4 | 8.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | 30% peg, 70 mM lithium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 25K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | drop | HEPES | 50 (mM) | |
3 | 1 | drop | 87.5 (mM) | ||
4 | 1 | drop | PEG6000 | 15 (%) | |
5 | 1 | reservoir | HEPES | 100 (mM) | |
6 | 1 | reservoir | 175 (mM) | ||
7 | 1 | reservoir | PEG6000 | 30 (%) |