9G51

Crystal structure of LmrR with V15 replaced by unnatural amino acid 4-mercaptophenylalanine, apo

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	2023-05-02
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.96546
Spacegroup name	C 1 2 1
Unit cell lengths	102.908, 34.988, 68.116
Unit cell angles	90.00, 97.18, 90.00

Refinement procedure

Resolution	67.580 - 2.350
R-factor	0.21936
Rwork	0.217
R-free	0.26238
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.989
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]	67.590	2.440
High resolution limit [Å]	2.350	2.350
Rmerge	0.044	1.273
Rmeas	0.050	1.447
Rpim	0.024	0.677
Total number of observations	45074	4622
Number of reflections	10311	1048
<I/σ(I)>	13.3	1
Completeness [%]	100.0
Redundancy	4.4	4.4
CC(1/2)	1.000	0.586

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		294	Sitting drops prepared with protein solution (14 mg/ml protein in 150 mM NaCl, 25 mM Tris-HCl, pH 7.5, 0.5 mM TCEP) mixed with reservoir crystallization solution (16-21% PEG 3350, 0.2 M KSCN in 0.2 M Bis-Tris propane, pH 6.5-7.2)