3PXB
Impact of BRCA1 BRCT domain missense substitutions on phospho-peptide recognition: T1700A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08ID-1 |
| Synchrotron site | CLSI |
| Beamline | 08ID-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-06-17 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97934 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 114.380, 114.380, 122.320 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 37.704 - 2.500 |
| R-factor | 0.2374 |
| Rwork | 0.235 |
| R-free | 0.27420 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1n5o |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.135 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.6.3_473)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 37.704 | 40.000 | 2.550 |
| High resolution limit [Å] | 2.500 | 4.000 | 2.500 |
| Number of reflections | 16748 | ||
| <I/σ(I)> | 14.7 | ||
| Completeness [%] | 99.1 | 99.5 | 99.8 |
| Redundancy | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 0.8 M Li2SO4 100 mM TRIS 5mM CaCl2 10 mM NiCl2, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
