7UP4

Crystal structure of C-terminal Domain of MSK1 in complex with covalently bound pyrrolopyrimidine compound 20 (co-crystal)

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	2021-04-08
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 21 21 21
Unit cell lengths	51.440, 91.180, 136.170
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.120 - 3.000
R-factor	0.1984
Rwork	0.191
R-free	0.27070
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	in-house model
RMSD bond length	0.004
RMSD bond angle	0.629
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHENIX
Refinement software	PHENIX (4205)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	3.080
High resolution limit [Å]	3.000	13.420	3.000
Rmerge	0.109	0.030	0.575
Rmeas	0.126	0.037	0.663
Number of reflections	13380	165	971
<I/σ(I)>	11.27	27.16	2.46
Completeness [%]	99.7	89.2	100
Redundancy	3.999	3.145	4.094
CC(1/2)	0.994	0.998	0.781

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	289	Crystals were produced by sitting drop vapor diffusion with an equal volume of the protein, Msk1-C terminal domain (PID7059-1, CID101276) at 7.6 mg/ml in 25mM HEPES pH 7.5, 150mM NaCl, 5% Glycerol, 5mM BME and a crystallization buffer containing 20mM of each DL-glutamic acid, DL-alanine, glycine, DL-lysine, DL-serine, sodium HEPES / MOPS (acid) pH 7.5, 12.5% (V/V) MPD, 12.5% (w/V) PEG 1000, 12.5% (w/V) PEG 3350 (tray ID 320260, well H8, Molecular Dimensions / Calibre Morpheus screen ). Crystals were direly vitrified in in liquid N2. Puck ID CNL6-3