4GPQ

Structural insights into inhibition of the bivalent menin-MLL interaction by small molecules in leukemia

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-D
Synchrotron site	APS
Beamline	21-ID-D
Detector technology	CCD
Detector	MARMOSAIC 300 mm CCD
Spacegroup name	P 21 21 21
Unit cell lengths	48.812, 80.178, 124.686
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	36.900 - 1.460
R-factor	0.14617
Rwork	0.145
R-free	0.17555
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3re2
RMSD bond length	0.016
RMSD bond angle	1.192
Refinement software	REFMAC (5.6.0119)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	36.900	1.490
High resolution limit [Å]	1.460	1.460
Number of reflections	85179
<I/σ(I)>	16.1	4.5
Completeness [%]	99.4	88.1
Redundancy	6.8	5.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5		0.2 M ammonium acetate, 0.1 M HEPES pH 7.5 and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl (pH 8.0), 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen, VAPOR DIFFUSION, SITTING DROP
1	VAPOR DIFFUSION, SITTING DROP	7.5		0.2 M ammonium acetate, 0.1 M HEPES pH 7.5 and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl (pH 8.0), 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen, VAPOR DIFFUSION, SITTING DROP