7CY0

Crystal structure of S185H mutant PET hydrolase from Ideonella sakaiensis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSRRC BEAMLINE BL15A1
Synchrotron site	NSRRC
Beamline	BL15A1
Temperature [K]	100
Detector technology	CCD
Collection date	2019-10-29
Detector	RAYONIX MX-300
Wavelength(s)	1.0
Spacegroup name	P 21 21 21
Unit cell lengths	50.925, 51.806, 84.287
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	24.710 - 1.320
R-factor	0.1451
Rwork	0.144
R-free	0.16560
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5xg0
RMSD bond length	0.010
RMSD bond angle	1.495
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.8.0266)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	25.000	25.000	1.370
High resolution limit [Å]	1.320	2.840	1.320
Rmerge	0.045	0.028	0.438
Rmeas	0.049	0.031	0.473
Rpim	0.018	0.011	0.176
Total number of observations	360092
Number of reflections	51200	5513	4970
<I/σ(I)>	14
Completeness [%]	96.7	98.6	95.5
Redundancy	7	7	7
CC(1/2)		0.999	0.933

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6	298	Polyethylene Glycol 6000, Glycerol, MES