7M6U

Crystal structure of a circular permutation and computationally designed pro-enzyme of carboxypeptidase G2

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007
Temperature [K]	93
Detector technology	IMAGE PLATE
Collection date	2017-06-06
Detector	RIGAKU RAXIS IV++
Wavelength(s)	1.54178
Spacegroup name	P 1 21 1
Unit cell lengths	78.540, 106.360, 121.930
Unit cell angles	90.00, 107.48, 90.00

Refinement procedure

Resolution	39.270 - 2.590
R-factor	0.22451
Rwork	0.222
R-free	0.27917
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1cg2
Data reduction software	xia2 (0.5.277-gc78b72c6-dials-1.5)
Data scaling software	xia2 (0.5.277-gc78b72c6-dials-1.5)
Phasing software	PHASER (2.7.17)
Refinement software	REFMAC (5.8.0258)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	39.270	39.250	2.630
High resolution limit [Å]	2.590	7.020	2.590
Rmerge	0.102	0.035	0.946
Rmeas	0.125	0.041	1.195
Rpim	0.071	0.022	0.719
Number of reflections	57919	2933	2833
<I/σ(I)>	6.8	19.5	0.9
Completeness [%]	97.2	95.6	95.77
Redundancy	2.9	3.21	2.48
CC(1/2)	0.952	0.998	0.388

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	293	Protein was prepared to a concentration of 19 mg/mL in 50 mM Tris 100 mM NaCl pH 7.4 0.2 mM ZnSO4. Reservoirs containing 750 uL of 20 mM Tris pH 8.0, 10% glycerol, and 10% PEG 3350 were prepared in 24 well hanging drop vapor diffusion plates. Equal volumes of protein solution and reservoir solution were mixed on a cover slip and suspended over the reservoir