Experiment: 2OM1

X-RAY DIFFRACTION

Starting Model(s)

Initial Refinement Model(s)
Type	Source	Accession Code	Details
experimental model	PDB	2OM0	insulin hexamer R6 conformation

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	6.5	291	15mM Na-SCN, 5%(v/v) ethanol, 200mM phosphate buffer, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K

Crystal Properties
Matthews coefficient	Solvent content
3.47	64.55

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 59	α = 90
b = 219.48	β = 90
c = 224.48	γ = 90

Symmetry
Space Group	C 2 2 21

Diffraction

Diffraction Experiment
ID #	Crystal ID	Scattering Type	Data Collection Temperature	Detector	Detector Type	Details	Collection Date	Monochromator	Protocol
1	1	x-ray	100	CCD	MARMOSAIC 225 mm CCD		2006-04-06	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	MAX II BEAMLINE I911-3	1.3	MAX II	I911-3

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	Net I Over Average Sigma (I)	Redundancy	Number Reflections (All)	Number Reflections (Observed)	Observed Criterion Sigma (F)	Observed Criterion Sigma (I)	B (Isotropic) From Wilson Plot
1	1.97	50	99.5	0.09	17.7	8.6	103274	102732			32.9

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	1.97	2	89.2		0.37	2.45	2.4	4480

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	Resolution (High)	Resolution (Low)	Number Reflections (Observed)	Number Reflections (R-Free)	Percent Reflections (Observed)	R-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	THROUGHOUT	insulin hexamer R6 conformation	1.97	19.99	97508	5132	99.5	0.17646	0.17463	0.21165	RANDOM	33.836

Temperature Factor Modeling
Anisotropic B[1][1]	Anisotropic B[1][2]	Anisotropic B[1][3]	Anisotropic B[2][2]	Anisotropic B[2][3]	Anisotropic B[3][3]

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.357
r_dihedral_angle_3_deg	13.205
r_dihedral_angle_4_deg	9.358
r_dihedral_angle_1_deg	9.055
r_scangle_it	3.988
r_scbond_it	2.47
r_mcangle_it	1.789
r_angle_refined_deg	1.408
r_mcbond_it	0.955
r_nbtor_refined	0.303

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.357
r_dihedral_angle_3_deg	13.205
r_dihedral_angle_4_deg	9.358
r_dihedral_angle_1_deg	9.055
r_scangle_it	3.988
r_scbond_it	2.47
r_mcangle_it	1.789
r_angle_refined_deg	1.408
r_mcbond_it	0.955
r_nbtor_refined	0.303
r_nbd_refined	0.235
r_symmetry_vdw_refined	0.211
r_xyhbond_nbd_refined	0.16
r_metal_ion_refined	0.158
r_symmetry_hbond_refined	0.155
r_chiral_restr	0.119
r_bond_refined_d	0.014
r_gen_planes_refined	0.006

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	7135
Nucleic Acid Atoms
Solvent Atoms	755
Heterogen Atoms	174

Software

Software
Software Name	Purpose
REFMAC	refinement
XDS	data reduction
XSCALE	data scaling
MOLREP	phasing

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.