3O2K

Crystal Structure of Brevianamide F Prenyltransferase Complexed with Brevianamide F and Dimethylallyl S-thiolodiphosphate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X06SA
Synchrotron site	SLS
Beamline	X06SA
Temperature [K]	100
Detector technology	PIXEL
Collection date	2009-12-04
Detector	PSI PILATUS 6M
Wavelength(s)	1.0000
Spacegroup name	P 41 21 2
Unit cell lengths	82.770, 82.770, 124.260
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.400
R-factor	0.20681
Rwork	0.205
R-free	0.23451
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3o24
RMSD bond length	0.005
RMSD bond angle	0.825
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	REFMAC
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.460
High resolution limit [Å]	2.400	2.400
Rmerge	0.042	0.228
Number of reflections	17518
<I/σ(I)>	29.95	8.61
Completeness [%]	99.9	100
Redundancy	23.6	27

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	298	1.3M ammonium sulfate, 0.2M lithium sulfate, 0.1M MES, VAPOR DIFFUSION, HANGING DROP. Stepwise transferred to 1.3M lithium sulfate, 0.1M MES pH 6.5, 2.5mM brevianamide F, 10mM dimethylallyl S-thiolodiphosphate for soaking, temperature 298K