4NIB

Crystal structure of human insulin mutant B20 D-ala, B23 D-ala

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	CCD
Collection date	2013-04-09
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.9537
Spacegroup name	I 21 3
Unit cell lengths	78.030, 78.030, 78.030
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	18.392 - 1.400
R-factor	0.1433
Rwork	0.141
R-free	0.16300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1b2a
RMSD bond length	0.009
RMSD bond angle	1.073
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHASER
Refinement software	PHENIX ((phenix.refine: 1.8.2_1309))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	20.000	1.500	1.350
High resolution limit [Å]	1.300	1.400	1.300
Number of reflections	19350
<I/σ(I)>		1.71	0.55
Completeness [%]	99.8	100	89.1
Redundancy	11.5	12.1	7.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	294	These insulin crystals were obtained from a co-crystallization experiment with insulin receptor fragment IR310.T. Crystals were formed in the presence of IR310.T as detailed for the IR310.T complex with native human insulin - in Menting et al. 2013, Nature 493:241-245. Crystallant was 0.7 M trisodium citrate, 0.1 M imidazole-HCl pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 294K