4WU3

Structure of the PTP-like myo-inositol phosphatase from Mitsuokella multacida in complex with myo-inositol-(1,3,4,5)-tetrakisphosphate

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	8	293	PEG 8000, Polyethylene glycol, Tris chloride, beta-mercapto ethanol, glycerol

Crystal Properties
Matthews coefficient	Solvent content
2.62	53.04

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 73.899	α = 107.27
b = 86.68	β = 91.69
c = 124.149	γ = 90.01

Symmetry
Space Group	P 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	RAYONIX MX-300		2011-02-04	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	CLSI BEAMLINE 08ID-1	.97934	CLSI	08ID-1

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	2.2	44.54	98.8	0.08	6	2.2		146418

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	2.2	2.24	96.6		0.16	4.3	2.2

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	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	MOLECULAR REPLACEMENT	THROUGHOUT	3F41	2.2	44.54	144299	2118	98.07	0.19014	0.18979	0.21341	RANDOM	19.523

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]
-0.13	-0.13	-0.13	-2.05	-0.66	2.18

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	33.849
r_dihedral_angle_4_deg	13.831
r_dihedral_angle_3_deg	12.264
r_dihedral_angle_1_deg	5.515
r_mcangle_it	2.804
r_mcbond_it	1.822
r_mcbond_other	1.82
r_angle_refined_deg	1.106
r_angle_other_deg	0.67
r_chiral_restr	0.057

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	33.849
r_dihedral_angle_4_deg	13.831
r_dihedral_angle_3_deg	12.264
r_dihedral_angle_1_deg	5.515
r_mcangle_it	2.804
r_mcbond_it	1.822
r_mcbond_other	1.82
r_angle_refined_deg	1.106
r_angle_other_deg	0.67
r_chiral_restr	0.057
r_bond_refined_d	0.007
r_gen_planes_refined	0.004
r_bond_other_d	0.002
r_gen_planes_other	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	19188
Nucleic Acid Atoms
Solvent Atoms	2262
Heterogen Atoms	270

Software

Software
Software Name	Purpose
REFMAC	refinement
MOLREP	phasing
Aimless	data scaling
MOSFLM	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 R01GM133198.