9RAQ

Apo crystal structure of a mutant of a computationally designed protein (TRP_F43W/E39L)

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	35.779, 59.727, 53.026
Unit cell angles	90.00, 93.17, 90.00

Refinement procedure

Resolution	52.940 - 2.104
Rwork	0.233
R-free	0.28490
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.732
Data reduction software	autoPROC
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (5.8.0425)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	52.940	2.170
High resolution limit [Å]	2.100	2.100
Number of reflections	11784	960
<I/σ(I)>	15.6
Completeness [%]	90.4
Redundancy	1.9
CC(1/2)	0.636	0.971

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		291	11.32 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.