6XP3

Structure of human PYCR1 complexed with cyclopentanecarboxylic acid

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 4.2.2
Synchrotron site	ALS
Beamline	4.2.2
Temperature [K]	100
Detector technology	CMOS
Collection date	2020-02-11
Detector	RDI CMOS_8M
Wavelength(s)	0.97625
Spacegroup name	C 1 2 1
Unit cell lengths	109.702, 178.533, 87.657
Unit cell angles	90.00, 106.85, 90.00

Refinement procedure

Resolution	47.175 - 1.930
R-factor	0.1906
Rwork	0.189
R-free	0.21880
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	2izz
Data reduction software	XDS
Data scaling software	Aimless (0.7.4)
Phasing software	PHENIX
Refinement software	PHENIX (1.14)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	47.180	47.180	1.960
High resolution limit [Å]	1.930	10.570	1.930
Rmerge	0.055	0.017	0.561
Rmeas	0.066	0.020	0.664
Rpim	0.035	0.010	0.350
Total number of observations	408772	2631	20160
Number of reflections	116598	735	5789
<I/σ(I)>	11.9	36.3	1.8
Completeness [%]	96.7	96.8	97.6
Redundancy	3.5	3.6	3.5
CC(1/2)	0.997	0.999	0.770

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	Reservoir contained 200 mM Li2SO4, 18% (w/v) PEG 3350, and 0.1 M HEPES at pH 7.5. Enzyme solution contained 10 mM cyclopentanecarboxylic acid. Crystal was soaked in cryobuffer containing 20% PEG 200, and 100 mM cyclopentanecarboxylic acid.