6V7G

Binding of Benzoic Acid and Anions Within the Cupin Domains of the Vicillin Protein Canavalin from Jack Bean (canavalia ensiformis): Crystal Structures

Replaces:  6CB4

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 8.3.1
Synchrotron site	ALS
Beamline	8.3.1
Temperature [K]	173
Detector technology	PIXEL
Collection date	2018-06-15
Detector	DECTRIS PILATUS3 R CdTe 300K
Wavelength(s)	1.0
Spacegroup name	P 63
Unit cell lengths	125.806, 125.806, 49.875
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	109.000 - 1.400
R-factor	0.1614
Rwork	0.160
R-free	0.18800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6CB4
RMSD bond length	0.010
RMSD bond angle	1.579
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (5.8.0253)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	109.000	1.430
High resolution limit [Å]	1.400	1.400
Rmerge	0.258
Rmeas	0.260
Rpim	0.029
Number of reflections	86853	3978
<I/σ(I)>	18.7	0.7
Completeness [%]	99.6	92.8
Redundancy	61	11.8
CC(1/2)	0.990	0.182

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6	298	Vapor diffusion in sitting drop Cryschem plates. Reservoirs were 1.0 M sodium citrate titrated with acetic acid to pH6.0. Drops were initially equal amounts of the reservoir solution with a protein stock solution of 30 mg/ml canavalin in water with a trace of ammonium hydroxide. At room temperature crystallization time was about three weeks.