7BB5

Crystal structure of anti-CRISPR protein AcrIF9

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Synchrotron site	PETRA III, EMBL c/o DESY
Beamline	P13 (MX1)
Temperature [K]	100
Detector technology	PIXEL
Collection date	2019-12-07
Detector	PSI PILATUS 6M
Wavelength(s)	0.976200
Spacegroup name	I 41 2 2
Unit cell lengths	77.285, 77.285, 75.663
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	54.649 - 2.300
R-factor	0.1866
Rwork	0.183
R-free	0.22270
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6VQV_A
RMSD bond length	0.003
RMSD bond angle	0.479
Data reduction software	XDS
Data scaling software	SCALA (3.3.20)
Phasing software	MOLREP (11.7.02)
Refinement software	PHENIX (1.12-2829)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	54.649	54.649	2.420
High resolution limit [Å]	2.300	7.270	2.300
Rmerge		0.065	0.461
Rmeas	0.145	0.069	0.474
Rpim	0.030	0.017	0.091
Total number of observations		4184	19637
Number of reflections	5344	207	752
<I/σ(I)>	17.4	24.5	9.3
Completeness [%]	99.9	100	99.8
Redundancy	24.9	20.2	26.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	291	Crystallization buffer was 0.1 M Tris-HCl pH 8.5, 3.0M NaCl