3ICK

Trypanosoma cruzi farnesyl diphosphate synthase homodimer in complex with minodronate and isopentenyl disphosphate

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	4.6	298	PEG 4000, 200mM Ammonium Sulfate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystal Properties
Matthews coefficient	Solvent content
2.31	46.71

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 58.1	�� = 90
b = 58.1	�� = 90
c = 390.567	�� = 120

Symmetry
Space Group	P 61 2 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	ADSC QUANTUM 315r		2005-10-31	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	NSLS BEAMLINE X29A	1.1	NSLS	X29A

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	2.4	50	92.2	0.09	8.4	8.9		15342

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	2.4	2.49	71		0.526		6.1	1115

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	FOURIER SYNTHESIS	THROUGHOUT	2.4	39.81	15221	772	92.15	0.184	0.181	0.259	RANDOM	39.03

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]
2.83	1.41		2.83		-4.24

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	39.598
r_dihedral_angle_4_deg	22.815
r_dihedral_angle_3_deg	18.407
r_dihedral_angle_1_deg	5.474
r_scangle_it	3.841
r_scbond_it	2.493
r_angle_refined_deg	1.861
r_mcangle_it	1.533
r_mcbond_it	0.906
r_nbtor_refined	0.31

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	39.598
r_dihedral_angle_4_deg	22.815
r_dihedral_angle_3_deg	18.407
r_dihedral_angle_1_deg	5.474
r_scangle_it	3.841
r_scbond_it	2.493
r_angle_refined_deg	1.861
r_mcangle_it	1.533
r_mcbond_it	0.906
r_nbtor_refined	0.31
r_symmetry_hbond_refined	0.278
r_symmetry_vdw_refined	0.27
r_nbd_refined	0.236
r_xyhbond_nbd_refined	0.235
r_chiral_restr	0.189
r_metal_ion_refined	0.032
r_bond_refined_d	0.017
r_gen_planes_refined	0.006

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2891
Nucleic Acid Atoms
Solvent Atoms	233
Heterogen Atoms	51

Software

Software
Software Name	Purpose
DENZO	data reduction
SCALEPACK	data scaling
REFMAC	refinement
PDB_EXTRACT	data extraction
HKL-2000	data reduction

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.