8VRE

Structure of PYCR1 complexed with NADH and N-formyl-L-proline

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-E
Synchrotron site	APS
Beamline	24-ID-E
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-11-02
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.979180
Spacegroup name	C 1 2 1
Unit cell lengths	110.529, 179.294, 88.360
Unit cell angles	90.00, 106.80, 90.00

Refinement procedure

Resolution	71.500 - 1.830
R-factor	0.1763
Rwork	0.175
R-free	0.20150
Structure solution method	FOURIER SYNTHESIS
RMSD bond length	0.008
RMSD bond angle	1.003
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHENIX (1.20.1_4487)
Refinement software	PHENIX ((1.20.1_4487: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	91.130	1.860
High resolution limit [Å]	1.830	1.830
Rmerge	0.070	0.882
Rmeas	0.081	1.022
Rpim	0.041	0.510
Total number of observations		27695
Number of reflections	267999	7109
<I/σ(I)>	10.8	1.4
Completeness [%]	98.2
Redundancy	3.8	3.9
CC(1/2)	0.998	0.572

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	Reservoir contained 340 mM Li2SO4, 20% (w/v) PEG 3350, and 0.1 M HEPES at pH 7.5. Enzyme solution contained 2 mM NADH and 4 mM N-formyl-L-proline (resuspended in DMSO). The final DMSO concentration was 4%. Crystal was soaked in cryobuffer containing 20% PEG 200 and 25 mM N-formyl-L-proline (resuspended in DMSO). The final DMSO concentration in the cryobuffer was 25%