3Q8T

Crystal structure of the coiled coil domain of Beclin 1, an essential autophagy protein

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	8.2	293	45% MPD, 2% PEG400, 100mM Tris, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystal Properties
Matthews coefficient	Solvent content
2.81	56.23

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 103.78	α = 90
b = 38.35	β = 97.92
c = 65.75	γ = 90

Symmetry
Space Group	C 1 2 1

Diffraction

Diffraction Experiment
ID #	Crystal ID	Scattering Type	Data Collection Temperature	Detector	Detector Type	Details	Collection Date	Monochromator	Protocol
1	1	x-ray	298	IMAGE PLATE	RIGAKU RAXIS IV++		2009-01-05	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	ROTATING ANODE	RIGAKU MICROMAX-007 HF	1.54

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (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	1.9	35.92	99.99			19438	19438	2	2

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	1.9	1.96	100

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	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	MIR	THROUGHOUT	1.9	35.92	19438	1062	100	0.21024	0.20876	0.23631	RANDOM	25.905

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]
-0.01		0.05	0.01		0.02

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.46
r_dihedral_angle_4_deg	19.803
r_dihedral_angle_3_deg	18.011
r_scangle_it	5.434
r_dihedral_angle_1_deg	3.627
r_scbond_it	3.529
r_mcangle_it	1.732
r_angle_refined_deg	1.243
r_mcbond_it	1.243
r_nbtor_refined	0.291

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.46
r_dihedral_angle_4_deg	19.803
r_dihedral_angle_3_deg	18.011
r_scangle_it	5.434
r_dihedral_angle_1_deg	3.627
r_scbond_it	3.529
r_mcangle_it	1.732
r_angle_refined_deg	1.243
r_mcbond_it	1.243
r_nbtor_refined	0.291
r_nbd_refined	0.243
r_xyhbond_nbd_refined	0.199
r_symmetry_hbond_refined	0.194
r_symmetry_vdw_refined	0.175
r_chiral_restr	0.091
r_bond_refined_d	0.014
r_gen_planes_refined	0.005

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1592
Nucleic Acid Atoms
Solvent Atoms	279
Heterogen Atoms

Software

Software
Software Name	Purpose
CrystalClear	data collection
MLPHARE	phasing
REFMAC	refinement
d*TREK	data reduction
d*TREK	data scaling

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.