8DB1

Crystal structure of native DMATS1 prenyltransferase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-C
Synchrotron site	APS
Beamline	24-ID-C
Temperature [K]	100
Detector technology	PIXEL
Collection date	2021-12-18
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	1
Spacegroup name	P 21 21 21
Unit cell lengths	89.644, 107.211, 178.984
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	91.970 - 2.720
R-factor	0.2215
Rwork	0.220
R-free	0.24660
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Alphafold
RMSD bond length	0.006
RMSD bond angle	0.987
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.14_3260)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	91.970	2.820
High resolution limit [Å]	2.720	2.720
Rmerge	0.147	1.290
Rpim	0.062	0.561
Number of reflections	46996	4548
<I/σ(I)>	10	1.6
Completeness [%]	99.7	99.8
Redundancy	6.6	6.3
CC(1/2)	0.995	0.514

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	294	7.5 mg/mL protein, 0.1 M Tris-HCl (pH 8.0), 0.7 M NaCl, 24% (v/v) PEG 3350