3F87

An alpha/beta-Peptide Helix Bundle with a Pure beta-Amino Acid Core and a Distinctive Quarternary Structure: GCN4pLI derivative with beta residues at a and d heptad positions - higher symmetry crystal

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	0.12 M NaI, 0.08 M NaCl, 0.1 M HEPES-Na pH 7.5, 20% (v/v) 2-methyl-2,4-pentanediol (MPD), VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystal Properties
Matthews coefficient	Solvent content
3.68	66.54

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 71.313	α = 90
b = 71.313	β = 90
c = 97.44	γ = 90

Symmetry
Space Group	P 43 21 2

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	BRUKER SMART 6000	confocal mirrors	2007-06-21	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	ROTATING ANODE	BRUKER AXS MICROSTAR	1.5418

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	R Sym 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	2.4	50.4	98.7	0.148	0.061		12.61	10451	10316

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	R-Sym I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	2.4	2.49	99.5		0.521	0.228	4.41	9.76	1096

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Resolution (High)	Resolution (Low)	Number Reflections (All)	Number Reflections (Observed)	Number Reflections (R-Free)	Percent Reflections (Observed)	R-Factor (All)	R-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	THROUGHOUT	2.4	50.4	9808	9808	490	99	0.233	0.233	0.23	0.296	RANDOM	17.868

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]
-0.14			-0.14		0.29

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	38.491
r_dihedral_angle_3_deg	18.282
r_dihedral_angle_4_deg	17.508
r_dihedral_angle_1_deg	6.543
r_scangle_it	3.785
r_scbond_it	2.181
r_angle_refined_deg	2.011
r_mcbond_other	1.478
r_angle_other_deg	1.393
r_mcangle_it	1.36

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	38.491
r_dihedral_angle_3_deg	18.282
r_dihedral_angle_4_deg	17.508
r_dihedral_angle_1_deg	6.543
r_scangle_it	3.785
r_scbond_it	2.181
r_angle_refined_deg	2.011
r_mcbond_other	1.478
r_angle_other_deg	1.393
r_mcangle_it	1.36
r_mcbond_it	0.67
r_chiral_restr	0.106
r_bond_other_d	0.026
r_bond_refined_d	0.013
r_gen_planes_refined	0.003
r_gen_planes_other	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1176
Nucleic Acid Atoms
Solvent Atoms	79
Heterogen Atoms	9

Software

Software
Software Name	Purpose
REFMAC	refinement
PROTEUM PLUS	data collection
PROTEUM PLUS	data reduction
PROTEUM PLUS	data scaling
PHASER	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 R01GM133198.