9G52

Crystal structure of LmrR with V15 replaced by unnatural amino acid 4-mercaptophenylalanine, Au(I) bound

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE MASSIF-1
Synchrotron site	ESRF
Beamline	MASSIF-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2023-11-05
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.96546
Spacegroup name	P 21 21 21
Unit cell lengths	35.440, 52.715, 146.194
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	42.790 - 2.500
R-factor	0.24783
Rwork	0.245
R-free	0.29397
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	1.817
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (5.8.0419)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.730	2.600
High resolution limit [Å]	2.500	2.500
Rmerge	0.120	1.340
Rmeas	0.127	1.427
Rpim	0.041	0.482
Total number of observations	94882	9546
Number of reflections	10107	1109
<I/σ(I)>	11.1	1.6
Completeness [%]	100.0
Redundancy	9.4	8.6
CC(1/2)	0.998	0.726

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	294	Sitting drops prepared with protein solution (0.412 mM protein, 0.824 mM KAuCN2, 20 mM MOPS, pH 7.0, 150 mM NaCl) and reservoir crystallization solution (0.2 M NaF, 0.1 M Bis-Tris propane, pH 7.5, 20% PEG 3350)