9N42

Crystal structure of an anti-CRISPR Protein AcrIE7

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-B
Synchrotron site	APS
Beamline	23-ID-B
Temperature [K]	90
Detector technology	PIXEL
Collection date	2023-04-03
Detector	DECTRIS EIGER X 16M
Wavelength(s)	1.034
Spacegroup name	C 1 2 1
Unit cell lengths	62.501, 62.077, 87.737
Unit cell angles	90.00, 103.21, 90.00

Refinement procedure

Resolution	85.416 - 1.500
Rwork	0.206
R-free	0.23680
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.016
RMSD bond angle	2.180
Data reduction software	DIALS
Data scaling software	Aimless (0.7.9)
Phasing software	PHASER (2.8.3)
Refinement software	REFMAC (5.8.0430 (refmacat 0.4.88))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	85.420	85.420	1.540
High resolution limit [Å]	1.500	11.620	1.510
Rmerge	0.073	0.066	2.813
Rmeas	0.075	0.067	2.880
Rpim	0.018	0.013	0.604
Number of reflections	51688	348	2164
<I/σ(I)>	21.8	52.6	1.2
Completeness [%]	98.7	0.998	98.7
Redundancy	32.7	28.7	21.5
CC(1/2)	0.999	0.997	0.696

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	293	22% PEG MME 5K, 0.1M BisTris (pH 5.4)