9QDH

Crystal structure of IgA protease (323-878) from Thomasclavelia ramosa

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I24
Synchrotron site	Diamond
Beamline	I24
Temperature [K]	100
Detector technology	PIXEL
Collection date	2024-04-27
Detector	DECTRIS EIGER2 X 9M
Wavelength(s)	0.61992
Spacegroup name	P 21 21 21
Unit cell lengths	70.739, 85.198, 90.666
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	55.770 - 2.000
R-factor	0.1965
Rwork	0.194
R-free	0.24480
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.003
RMSD bond angle	0.623
Data reduction software	xia2
Data scaling software	xia2
Phasing software	PHASER
Refinement software	PHENIX ((1.20.1_4487: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	55.770	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.346	2.869
Rpim	0.098	0.847
Number of reflections	37731	3740
<I/σ(I)>	5.91	0.83
Completeness [%]	100.0	100
Redundancy	13.4	12.5
CC(1/2)	0.994	0.534

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	291	25% PEG 3350, 0.1M Tris pH 8.5, 0.2M NaCl and VPCPVPSTPP peptide 5mM. Cryoprotectant solution: 30% glycerol, 27% PEG 3350, 0.1M Tris pH 8.5 and 0.2M NaCl. Protein:precipitant ratio 1:1. Protein concentration: 12.2 mg/ml. Protein buffer: 20mM Tris pH 7.5.