4FBD

2.35 Angstrom Crystal Structure of Conserved Hypothetical Protein from Toxoplasma gondii ME49.

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	7	295	Protein: 7.0mg/mL, 0.5M Sodium cloride, Tris-HCl pH 8.3; Screen: JCSG+ (F11), 1M Succinic acid pH 7.0, 0.1M HEPES pH 7.0, 1.0% (w/v) PEG MME 2000; Cryo: Screen solution : 50% Sucrose, 1:1 (v/v), VAPOR DIFFUSION, SITTING DROP, temperature 295K

Crystal Properties
Matthews coefficient	Solvent content
2.15	42.69

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 47.599	α = 90
b = 87.216	β = 90
c = 112.122	γ = 90

Symmetry
Space Group	P 21 21 21

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	MARMOSAIC 225 mm CCD	Beryllium lenses	2011-10-12	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 21-ID-F	0.97872	APS	21-ID-F

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	2.35	30	100	0.066	27.6	7.3	20165	20165		-3	58.5

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	2.35	2.39	100		0.557	3.9	7.2	983

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	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	2PD0	2.35	29.4	19076	19076	1026	99.96	0.20509	0.20509	0.20232	0.25826	RANDOM	53.823

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]
-0.51			1.53		-1.02

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	22.658
r_dihedral_angle_3_deg	11.99
r_dihedral_angle_4_deg	10.074
r_scangle_it	4.433
r_scbond_it	3.053
r_dihedral_angle_1_deg	2.609
r_mcangle_it	2.223
r_angle_refined_deg	1.471
r_mcbond_it	1.235
r_angle_other_deg	0.851

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	22.658
r_dihedral_angle_3_deg	11.99
r_dihedral_angle_4_deg	10.074
r_scangle_it	4.433
r_scbond_it	3.053
r_dihedral_angle_1_deg	2.609
r_mcangle_it	2.223
r_angle_refined_deg	1.471
r_mcbond_it	1.235
r_angle_other_deg	0.851
r_mcbond_other	0.289
r_chiral_restr	0.092
r_bond_refined_d	0.013
r_gen_planes_refined	0.006
r_bond_other_d	0.001
r_gen_planes_other	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	3172
Nucleic Acid Atoms
Solvent Atoms	98
Heterogen Atoms

Software

Software
Software Name	Purpose
Blu-Ice	data collection
PHENIX	model building
REFMAC	refinement
HKL-2000	data reduction
HKL-2000	data scaling
PHENIX	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.