2FPB

Structure of Strictosidine Synthase, the Biosynthetic Entry to the Monoterpenoid Indole Alkaloid Family

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION	7.5	295	0.8M potassium sodium tartrate tetrahydrate, 100mM HEPES-Na, 1mM Tryptamine, pH 7.5, VAPOR DIFFUSION, temperature 295.0K

Crystal Properties
Matthews coefficient	Solvent content
3.58	65.68

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 148.936	α = 90
b = 148.936	β = 90
c = 121.344	γ = 120

Symmetry
Space Group	H 3

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	MARRESEARCH	double crystal Si[111]	2004-03-14	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	EMBL/DESY, HAMBURG BEAMLINE BW7A	0.9714	EMBL/DESY, HAMBURG	BW7A

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	2.8	20	99.9	0.099	3	3	24731	23380	2	2	44

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	2.8	2.84	100		0.436	3

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Resolution (High)	Resolution (Low)	Cut-off Sigma (F)	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	2.8	20	2	23380	1253	99.9	0.17	0.16631	0.16363	0.21717	RANDOM	23.105

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]
4.54	2.27		4.54		-6.81

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_1_deg	7.152
r_scangle_it	5.054
r_scbond_it	3.33
r_angle_refined_deg	1.707
r_mcangle_it	1.332
r_mcbond_it	0.676
r_symmetry_vdw_refined	0.296
r_nbd_refined	0.234
r_xyhbond_nbd_refined	0.167
r_chiral_restr	0.113

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_1_deg	7.152
r_scangle_it	5.054
r_scbond_it	3.33
r_angle_refined_deg	1.707
r_mcangle_it	1.332
r_mcbond_it	0.676
r_symmetry_vdw_refined	0.296
r_nbd_refined	0.234
r_xyhbond_nbd_refined	0.167
r_chiral_restr	0.113
r_bond_refined_d	0.018
r_gen_planes_refined	0.006

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	4810
Nucleic Acid Atoms
Solvent Atoms	173
Heterogen Atoms	24

Software

Software
Software Name	Purpose
REFMAC	refinement
MAR345	data collection
SCALEPACK	data scaling
MOLREP	phasing

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.