9RAR

Apo crystal structure of a mutant of a computationally designed protein (TRP_F43W)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I04
Synchrotron site	Diamond
Beamline	I04
Temperature [K]	100
Detector technology	PIXEL
Collection date	2025-02-26
Detector	DECTRIS EIGER2 XE 16M
Wavelength(s)	0.9763
Spacegroup name	P 1 21 1
Unit cell lengths	36.089, 60.094, 53.783
Unit cell angles	90.00, 93.60, 90.00

Refinement procedure

Resolution	53.680 - 1.750
Rwork	0.230
R-free	0.28480
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.733
Data reduction software	xia2
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (5.8.0425)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	53.680	1.780
High resolution limit [Å]	1.750	1.750
Number of reflections	23131	1274
<I/σ(I)>	13.4	2.7
Completeness [%]	99.5
Redundancy	3.7
CC(1/2)	0.579	0.862

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		291	11.23 mgmL-1 TRP (in 20 mM MES pH 5.2, 150 mM NaCl) was pipetted into an MRC 3-well plate in a 1:2 ratio TRP:mother liquor, where mother liquor = 1% (w/v) tryptone, 0.05 M HEPES pH 7, 12% (w/v) PEG 3350. Crystals grew after 1-2 days.