2OMH

Structure of human insulin cocrystallized with ARG-12 peptide in presence of urea

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I911-2
Synchrotron site	MAX II
Beamline	I911-2
Temperature [K]	100
Detector technology	CCD
Collection date	2004-10-07
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	1.0
Spacegroup name	P 43 21 2
Unit cell lengths	61.360, 61.360, 85.600
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	14.950 - 1.360
R-factor	0.20136
Rwork	0.200
R-free	0.22274
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	insulin trimer R conformation
RMSD bond length	0.008
RMSD bond angle	1.112
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.400
High resolution limit [Å]	1.360	1.360
Rmerge	0.058	0.610
Number of reflections	34738
<I/σ(I)>	12.3	2.2
Completeness [%]	96.9	98.8
Redundancy	5.3	4.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.3	291	500mM NaCl, 2.5M urea, 1.2mg/ml ARG-12 peptide, 50mM resorcinol, 50mM phosphate buffer, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 291K