4EDU
The MBT repeats of human SCML2 in a complex with histone H2A peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-07-26 |
| Detector | ADSC Q315 |
| Wavelength(s) | 0.97937 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 69.949, 69.949, 169.609 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 2.580 |
| R-factor | 0.206 |
| Rwork | 0.204 |
| R-free | 0.24500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1oi1 |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.463 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 43.970 | 43.970 | 2.720 |
| High resolution limit [Å] | 2.580 | 8.160 | 2.580 |
| Rmerge | 0.111 | 0.030 | 0.980 |
| Rmeas | 0.030 | 1.050 | |
| Total number of observations | 3348 | 15670 | |
| Number of reflections | 15321 | ||
| <I/σ(I)> | 15.5034 | ||
| Completeness [%] | 99.9 | 98.95 | 99.95 |
| Redundancy | 7.71 | 6.31 | 7.92 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 9.5 | 291 | 1.6M NH4PO4, 0.1M Tris/HCl, 1:5 molar ratio of protein:peptide, protein concentration 35 mg/ml, pH 9.5, vapor diffusion, hanging drop, temperature 291K |






