8DB0

Crystal structure of DMATS1 prenyltransferase in complex with L-Trp and DMSPP

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	2021-10-09
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	0.979
Spacegroup name	P 21 21 21
Unit cell lengths	90.500, 108.400, 182.040
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	93.140 - 2.260
R-factor	0.2068
Rwork	0.206
R-free	0.23240
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Alphafold
RMSD bond length	0.005
RMSD bond angle	0.778
Data reduction software	iMOSFLM
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.14_3260)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	93.140	2.300
High resolution limit [Å]	2.260	2.260
Rmerge	0.210	2.190
Rpim	0.079	1.260
Number of reflections	84491	4417
<I/σ(I)>	7.4	2.2
Completeness [%]	100.0	99.9
Redundancy	7.8
CC(1/2)	0.995	0.520

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.9	294	7.5 mg/mL protein, 0.1 M Tris-HCl (pH 8.9), 0.55 M NaCl, 25% (v/v) PEG 3,350