7MYB

Structure of proline utilization A with tetrahydrothiophene-2-carboxylate bound in the proline dehydrogenase active site

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	2019-11-02
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	0.979100
Spacegroup name	P 1 21 1
Unit cell lengths	101.884, 103.024, 127.062
Unit cell angles	90.00, 106.44, 90.00

Refinement procedure

Resolution	97.720 - 1.520
R-factor	0.165
Rwork	0.164
R-free	0.18600
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	5kf6
Data reduction software	XDS
Data scaling software	Aimless (0.5.32)
Phasing software	PHENIX
Refinement software	PHENIX (1.14)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	103.020	1.540
High resolution limit [Å]	1.518	1.520
Rmerge	0.066	0.492
Number of reflections	383136	18385
<I/σ(I)>	17.8
Completeness [%]	99.1	96.1
Redundancy	3.8	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	286	Protein stock solution: 6 mg/mL PutA with 50 mM tetrahydrothiophene-2-carboxylate in a buffer containing 50 mM Tris (pH 8.0), 50 mM NaCl, 5% (w/v) glycerol, and 0.5 mM Tris(2-caboxyethyl)phosphine. Reservoir solution: 19 % PEG-3350, 0.2 M ammonium sulfate, 0.1 M magnesium chloride, 0.1 M HEPES (pH 8.0), and 0.1 M sodium formate. Cryo-buffer: reservoir supplemented with 15 % PEG-200. Crystals were grown and harvested in low-light conditions