7NMI
Transactivation domain of p53 in complex with S100P, using annexin A2 as crystallization chaperone
Experimental procedure
| Experimental method | SINGLE WAVELENGTH | 
| Source type | SYNCHROTRON | 
| Source details | SLS BEAMLINE X06SA | 
| Synchrotron site | SLS | 
| Beamline | X06SA | 
| Temperature [K] | 100 | 
| Detector technology | PIXEL | 
| Collection date | 2020-12-17 | 
| Detector | DECTRIS EIGER X 16M | 
| Wavelength(s) | 1 | 
| Spacegroup name | P 21 21 21 | 
| Unit cell lengths | 65.920, 86.770, 113.420 | 
| Unit cell angles | 90.00, 90.00, 90.00 | 
Refinement procedure
| Resolution | 47.636 - 2.100 | 
| R-factor | 0.1958 | 
| Rwork | 0.194 | 
| R-free | 0.22760 | 
| Structure solution method | MOLECULAR REPLACEMENT | 
| Starting model (for MR) | 1xjl | 
| Data reduction software | XDS | 
| Data scaling software | XSCALE | 
| Phasing software | PHASER | 
| Refinement software | PHENIX (1.16_3549) | 
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 47.636 | 47.636 | 2.150 | 
| High resolution limit [Å] | 2.100 | 9.390 | 2.100 | 
| Rmerge | 0.126 | 0.035 | 1.165 | 
| Rmeas | 0.132 | 0.037 | 1.242 | 
| Total number of observations | 450497 | ||
| Number of reflections | 38715 | 510 | 2821 | 
| <I/σ(I)> | 22.47 | 69.26 | 3.02 | 
| Completeness [%] | 99.9 | 98.6 | 99.8 | 
| Redundancy | 11.636 | 11.661 | 9.359 | 
| CC(1/2) | 0.998 | 0.999 | 0.528 | 
Crystallization Conditions
| crystal ID | method | pH | temperature | details | 
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | Morpheus screen (MD) H6 0.1 M Amino acids, 0.1 M Buffer System 2, pH 7.5, 30 % v/v Precipitant Mix 2 | 











