3EMU

Crystal structure of a leucine rich repeat and phosphatase domain containing protein from Entamoeba histolytica

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION	7	294	500mM ammonium sulfate, 1M lithium sulfate, 100mM tri-sodium citrate dihydrate, pH 7.0, Vapor diffusion, temperature 294K, VAPOR DIFFUSION

Crystal Properties
Matthews coefficient	Solvent content
4.67	73.64

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 80.985	α = 90
b = 80.985	β = 90
c = 90.556	γ = 120

Symmetry
Space Group	P 31 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	100	CCD	MARMOSAIC 225 mm CCD		2008-09-12	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	CLSI BEAMLINE 08ID-1	0.97958	CLSI	08ID-1

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	R Sym 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	2.3	38.042	100	0.077	0.077	15.2	9.8	15704	15704			57.6

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	R-Sym I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
	2.3	2.42	100		0.453	0.453	3.7	9.9	2252

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Resolution (High)	Resolution (Low)	Number Reflections (All)	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	SAD	THROUGHOUT	2.3	20	15641	15641	748	100	0.23	0.23	0.236	RANDOM	65.638

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]
0.93	0.46		0.93		-1.39

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.943
r_dihedral_angle_4_deg	19.429
r_dihedral_angle_3_deg	16.369
r_dihedral_angle_1_deg	6.266
r_scangle_it	4.635
r_scbond_it	2.849
r_mcangle_it	1.885
r_angle_refined_deg	1.553
r_mcbond_it	0.979
r_chiral_restr	0.109

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.943
r_dihedral_angle_4_deg	19.429
r_dihedral_angle_3_deg	16.369
r_dihedral_angle_1_deg	6.266
r_scangle_it	4.635
r_scbond_it	2.849
r_mcangle_it	1.885
r_angle_refined_deg	1.553
r_mcbond_it	0.979
r_chiral_restr	0.109
r_bond_refined_d	0.018
r_gen_planes_refined	0.009

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1148
Nucleic Acid Atoms
Solvent Atoms	33
Heterogen Atoms	5

Software

Software
Software Name	Purpose
SCALA	data scaling
REFMAC	refinement
PDB_EXTRACT	data extraction
MA	data collection
MOSFLM	data reduction
SHELXCD	phasing
SHELXE	model building

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.