3ICZ

Trypanosoma cruzi farnesyl diphosphate synthase homodimer in complex with 1-(2,2-Bis-phosphono-ethyl)-3-butyl-pyridinium and isopentenyl pyrophosphate

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
2.34	47.42

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 58.398	�� = 90
b = 58.398	�� = 90
c = 391.809	�� = 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	MAR CCD 165 mm		2008-07-15	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 31-ID	0.97929	APS	31-ID

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	2.15	50	93.4	0.096	9	10.6		21604

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	2.15	2.23	73.4		0.227		5	1627

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	2.15	44.94	21411	1099	93.14	0.191	0.188	0.257	RANDOM	36.069

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]
1.84	0.92		1.84		-2.77

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	39.474
r_dihedral_angle_4_deg	19.826
r_dihedral_angle_3_deg	16.433
r_dihedral_angle_1_deg	5.477
r_scangle_it	4.46
r_scbond_it	3.01
r_angle_refined_deg	1.784
r_mcangle_it	1.707
r_mcbond_it	1.171
r_nbtor_refined	0.309

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	39.474
r_dihedral_angle_4_deg	19.826
r_dihedral_angle_3_deg	16.433
r_dihedral_angle_1_deg	5.477
r_scangle_it	4.46
r_scbond_it	3.01
r_angle_refined_deg	1.784
r_mcangle_it	1.707
r_mcbond_it	1.171
r_nbtor_refined	0.309
r_symmetry_hbond_refined	0.257
r_symmetry_vdw_refined	0.235
r_nbd_refined	0.231
r_xyhbond_nbd_refined	0.2
r_chiral_restr	0.124
r_bond_refined_d	0.021
r_metal_ion_refined	0.017
r_gen_planes_refined	0.008

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2891
Nucleic Acid Atoms
Solvent Atoms	295
Heterogen Atoms	37

Software

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

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.