9E0C

Structure of proline utilization A complexed with 1-benzofuran-5-ylmethanol

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 8.2.1
Synchrotron site	ALS
Beamline	8.2.1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2023-12-16
Detector	DECTRIS EIGER2 S 9M
Wavelength(s)	1.00009
Spacegroup name	P 1 21 1
Unit cell lengths	100.369, 101.642, 125.924
Unit cell angles	90.00, 106.42, 90.00

Refinement procedure

Resolution	48.140 - 1.320
R-factor	0.1733
Rwork	0.172
R-free	0.19040
Structure solution method	FOURIER SYNTHESIS
RMSD bond length	0.006
RMSD bond angle	0.899
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.21rc1_5156)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.140	1.340
High resolution limit [Å]	1.320	1.320
Rmerge	0.060	1.757
Rmeas	0.065	1.975
Rpim	0.025	0.884
Total number of observations		80388
Number of reflections	1044248	16856
<I/σ(I)>	14.1	0.7
Completeness [%]	93.9
Redundancy	6.7	4.8
CC(1/2)	0.999	0.369

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	Reservoir contained 0.1 M HEPES, pH 7.5, 0.1 M sodium formate, 0.1 M magnesium chloride, 0.2 M ammonium sulfate, and 18% (w/v) PEG 3350. Enzyme was incubated with 24 mM 1-benzofuran-5-ylmethanol. Crystal was soaked in cryobuffer containing 50 mM 1-benzofuran-5-ylmethanol and 20% PEG 200