6OS6

Crystal structure of CymD prenyltransferase complexed with L-tryptophan and DMSPP

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS-II BEAMLINE 17-ID-2
Synchrotron site	NSLS-II
Beamline	17-ID-2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2019-03-01
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.97932
Spacegroup name	I 4
Unit cell lengths	129.446, 129.446, 49.777
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.118 - 1.330
R-factor	0.1665
Rwork	0.166
R-free	0.18090
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Author used SWISS-MODEL server to generate a phasing model based on the protein sequence. SWISS-MODEL produced a phasing model based on PDB Entry 5JXM. Author used the polyALA version of the model for phasing.
Data reduction software	XDS
Data scaling software	Aimless (0.5.21)
Phasing software	PHASER
Refinement software	PHENIX (1.13_2998)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	29.120	29.120	1.360
High resolution limit [Å]	1.330	5.940	1.330
Rmerge	0.070	0.041	0.685
Rmeas	0.075	0.044	0.739
Rpim	0.027	0.016	0.275
Total number of observations	708407	8190	47653
Number of reflections	95021	1123	6812
<I/σ(I)>	15	44.2	2.3
Completeness [%]	99.8	99.2	97.3
Redundancy	7.5	7.3	7
CC(1/2)	0.999	0.998	0.806

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		294	1% (w/v) tryptone, 0.05 M HEPES-Na (pH 7.0), 12% PEG 3350