5UAU

Structure of human PYCR-1 complexed with proline

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	2015-10-18
Detector	RDI CMOS_8M
Wavelength(s)	1.00
Spacegroup name	P 21 21 2
Unit cell lengths	165.130, 87.750, 117.130
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	64.626 - 1.900
R-factor	0.1978
Rwork	0.196
R-free	0.22830
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2izz
RMSD bond length	0.005
RMSD bond angle	0.699
Data reduction software	XDS
Data scaling software	Aimless (0.5.15)
Phasing software	PHASER
Refinement software	PHENIX ((1.10.1_2155))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	64.630	64.630	1.930
High resolution limit [Å]	1.900	10.410	1.900
Rmerge	0.105	0.041	0.899
Rmeas		0.043	0.971
Rpim		0.013	0.366
Total number of observations		10769	45238
Number of reflections	133932
<I/σ(I)>	10.6	62.3	1.5
Completeness [%]	99.7	99.3	99.9
Redundancy	7.4	11.4	6.9
CC(1/2)	0.997	0.999	0.846

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	295	300 mM Na2SO4, 16-18% (w/v) polyethylene glycol (PEG) 3350, and 0.1 M HEPES at pH 7.5. The crystal was soaked in 1.8 M L-proline