6XP0

Structure of human PYCR1 complexed with 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	2018-03-16
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.9792
Spacegroup name	P 21 21 2
Unit cell lengths	164.630, 88.513, 115.462
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	67.026 - 1.950
R-factor	0.1873
Rwork	0.187
R-free	0.20910
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	5uau
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]	82.320	82.320	1.980
High resolution limit [Å]	1.950	10.680	1.950
Rmerge	0.080	0.039	1.304
Rmeas	0.094	0.046	1.525
Rpim	0.048	0.023	0.774
Total number of observations	435036	2807	22723
Number of reflections	120287	802	6045
<I/σ(I)>	7.2	21.3	0.8
Completeness [%]	97.8	93.9	99.7
Redundancy	3.6	3.5	3.8
CC(1/2)	0.996	0.996	0.483

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		295	Crystallization reservoir contained 250 mM Li2SO4, 19% (w/v) PEG 3350, and 0.1 M HEPES at pH 7.5. Crystal was soaked in cryobuffer containing 100 mM N-formyl L-proline and 20% PEG 200.