9HUD

Alpha-1-antitrypsin in the cleaved conformation in complex with a conformationally nonselective Fab fragment

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID30B
Synchrotron site	ESRF
Beamline	ID30B
Temperature [K]	100
Detector technology	PIXEL
Collection date	2024-08-31
Detector	DECTRIS EIGER R 4M
Wavelength(s)	0.9677
Spacegroup name	P 21 21 2
Unit cell lengths	117.254, 239.246, 68.945
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.650 - 2.420
R-factor	0.2132
Rwork	0.211
R-free	0.24720
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.003
RMSD bond angle	0.572
Data reduction software	XDS (Jun 30, 2024)
Data scaling software	Aimless (0.7.13)
Phasing software	PHASER (2.8.3)
Refinement software	PHENIX (1.21.2_5419)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	47.830	2.470
High resolution limit [Å]	2.420	2.420
Rmerge	0.317	3.242
Rmeas	0.332	3.388
Rpim	0.098	0.976
Total number of observations	845424	54265
Number of reflections	74867	4594
<I/σ(I)>	8.5	0.9
Completeness [%]	99.9
Redundancy	11.3	11.8
CC(1/2)	0.993	0.326

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	293	0.1M sodium HEPES, MOPS 0.1M DL-Glutamic acid monohydrate; 0.1M DL-Alanine; 0.1M Glycine; 0.1M DL-Lysine 40% v/v Glycerol; 20% w/v PEG 4000