6VET

Human insulin analog: [GluB10,HisA8,ArgA9,TyrB20]-DOI

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Synchrotron site	Australian Synchrotron
Beamline	MX2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-11-03
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.9537
Spacegroup name	P 21 21 21
Unit cell lengths	28.371, 52.117, 80.499
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	43.749 - 1.460
R-factor	0.2049
Rwork	0.201
R-free	0.23760
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Editted version of 6VER
RMSD bond length	0.006
RMSD bond angle	0.610
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((1.13-2998_1692))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	43.750	1.480
High resolution limit [Å]	1.460	1.460
Rmerge	0.143	4.470
Rmeas	0.149	4.653
Rpim	0.041	1.273
Number of reflections	21579	1000
<I/σ(I)>	9.7	0.6
Completeness [%]	99.5	90.4
Redundancy	13	12.5
CC(1/2)	0.999	0.380

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	300	Well condition: 0.3 M magnesium formate plus 0.1 M TrisHCl. Protein: The insulin analog was prepared in a mixture that also contained receptor fragments: 5 mg/ml (IR310.T).Fv83-7 in 10mM HEPES-NaOH (pH7.5) + 0.02% NaN3 plus three mol equivalents of the IR-A alphaCT peptide 704-719 plus 1.8 mol equivalents of the analog. The analog crystallized in isolation from the receptor fragments and it is not known whether the receptor fragments aided crystallization