9BR3

Crystal structure of p53 Y220C mutant in complex with PC-10709

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2016-11-09
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 21 21 21
Unit cell lengths	64.960, 71.210, 104.850
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.991 - 1.900
R-factor	0.1537
Rwork	0.152
R-free	0.19100
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	0.829
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHENIX
Refinement software	PHENIX (1.11.1_2575)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	47.991	47.991	1.950
High resolution limit [Å]	1.900	8.500	1.900
Rmerge	0.098	0.034	0.390
Rmeas	0.107	0.038	0.432
Total number of observations	232344
Number of reflections	38106	503	2297
<I/σ(I)>	14.91	32.86	4.17
Completeness [%]	97.6	98.4	81.1
Redundancy	6.097	5.171	5.34
CC(1/2)	0.998	0.998	0.933

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		289	p53, CID 3799, at 6.93mg/ml; Optimization screen PMV1-opt1 e3: 16% PEG 8000, 20% glycerol, 20mM K2HPO4; protein + 1mM BSI 107743; cryo: direct; crystal tracking ID 285723e3, puck tai0-7