9O4M

Crystal structure of Ubiquitin Carboxy Terminal Hydrolase L1 Q209C mutant covalently crosslinked to ubiquitin genetically encoded with N6-(6-bromohexanoyl)-L-lysine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	PIXEL
Collection date	2024-04-10
Detector	DECTRIS EIGER2 R 4M
Wavelength(s)	1.54184
Spacegroup name	P 32 2 1
Unit cell lengths	93.867, 93.867, 140.330
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.930 - 2.000
R-factor	0.226
Rwork	0.224
R-free	0.26200
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.002
RMSD bond angle	0.439
Data reduction software	CrysalisPro
Data scaling software	CrysalisPro
Phasing software	PHENIX
Refinement software	PHENIX ((1.20.1_4487: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	140.330	2.070
High resolution limit [Å]	2.000	2.000
Rmerge		0.835
Number of reflections	48911	4906
<I/σ(I)>	16.91	1.02
Completeness [%]	99.8	100
Redundancy	10.3	9.8
CC(1/2)	0.998	0.926

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	293	2.1 M DL-Malic acid