9RAA

Apo crystal structure of a computationally designed protein (TRP)

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	2025-02-02
Detector	DECTRIS EIGER2 X 16M
Wavelength(s)	0.9763
Spacegroup name	P 1 21 1
Unit cell lengths	36.134, 60.330, 54.083
Unit cell angles	90.00, 93.19, 90.00

Refinement procedure

Resolution	54.060 - 2.100
Rwork	0.214
R-free	0.27160
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.833
Data reduction software	DIALS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (5.8.0425)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	60.330	2.160
High resolution limit [Å]	2.100	2.100
Number of reflections	13564	1119
<I/σ(I)>	14.1
Completeness [%]	99.1
Redundancy	1.9
CC(1/2)	0.996	0.916

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		291	9.76 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.