6JLS

Crystal Structure of FMN-dependent Cysteine Decarboxylases TvaF from Thioviridamide Biosynthesis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRF BEAMLINE BL18U1
Synchrotron site	SSRF
Beamline	BL18U1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2018-10-26
Detector	DECTRIS PILATUS3 S 6M
Wavelength(s)	0.9793
Spacegroup name	F 41 3 2
Unit cell lengths	216.915, 216.915, 216.915
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	76.691 - 2.240
R-factor	0.2166
Rwork	0.216
R-free	0.23150
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1g63
RMSD bond length	0.007
RMSD bond angle	0.890
Data reduction software	MOSFLM
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((1.14_3235: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	76.691	2.310
High resolution limit [Å]	2.240	2.240
Number of reflections	21611	1937
<I/σ(I)>	11.5
Completeness [%]	100.0
Redundancy	29.8
CC(1/2)	0.999	0.395

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		295	Two micro liters of protein solution containing 7 mg/ml Tvaf in 20 mM Tris, pH 8.0, 50 mM NaCl, was mixed with 2 micro liters of well solution containing 0.1 M Sodium chloride, 0.1M Bicine pH 9.0, and 30% PEG 500 MME (vol/vol). The crystallization drop was incubated against 100 micro liters of well solution.