5W8F

Crystal structure of human Mcl-1 in complex with modified Bim BH3 peptide SAH-MS1-14

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-E
Synchrotron site	APS
Beamline	24-ID-E
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-04-14
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.97918
Spacegroup name	P 41 21 2
Unit cell lengths	46.850, 46.850, 167.440
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.620 - 1.850
R-factor	0.244
Rwork	0.242
R-free	0.28900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3mk8
RMSD bond length	0.007
RMSD bond angle	0.719
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX ((1.11.1_2575: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.615	1.900
High resolution limit [Å]	1.850	1.850
Rmerge	0.081	1.850
Number of reflections	16798
<I/σ(I)>	14.48	1.3
Completeness [%]	99.8	99.9
Redundancy	11.84	11.85
CC(1/2)		0.674

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	9	300	Reservior : 25% PEG 3350, 50mM Tris pH 9.0, 0.2 M Ammonium acetate; Protein: 408 uM in 20 mM TRis , 10 mM TCEP, 5mM Zn2SO4