9GVF

Crystal structure of a computationally designed protein

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X06SA
Synchrotron site	SLS
Beamline	X06SA
Temperature [K]	100
Detector technology	PIXEL
Collection date	2023-09-04
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.9999
Spacegroup name	P 1 21 1
Unit cell lengths	36.281, 60.375, 54.517
Unit cell angles	90.00, 93.42, 90.00

Refinement procedure

Resolution	40.420 - 1.600
Rwork	0.207
R-free	0.25180
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.810
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (5.8.0425)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.420	1.630
High resolution limit [Å]	1.600	1.600
Rmerge	0.032	0.359
Rmeas	0.039
Rpim	0.021	0.224
Number of reflections	30949	1519
<I/σ(I)>	12.9	2.4
Completeness [%]	99.6	99.8
Redundancy	3.4	3.5
CC(1/2)	0.998	0.875

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	Protein purified in MES pH 5.2, 150 mM NaCl (5 mgmL-1) Incubated in a 1:1 ratio with 0.2 M Sodium malonate pH 7.0, 20% w/v Polyethylene glycol 3,35 (E8 PEG-Ion HT) Reservoir: 0.2 M Sodium malonate pH 7.0, 20% w/v Polyethylene glycol 3,35 (E8 PEG-Ion HT)