3OGA

1.75 Angstrom resolution crystal structure of a putative NTP pyrophosphohydrolase (yfaO) from Salmonella typhimurium LT2

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	4.5	293	8 mg/mL protein in 10 mM Tris/HCl pH 8.3, 500 mM NaCl, 5 mM BME. Crystallization condition: The JCSG+ suite condition 56 (1 M di-Ammonium phosphate 0.1 M Sodium acetate pH 4.5), VAPOR DIFFUSION, SITTING DROP, temperature 293K

Crystal Properties
Matthews coefficient	Solvent content
2.43	49.48

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 41.589	α = 90
b = 81.104	β = 90
c = 110.075	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	Be-Lenses/Diamond Laue Mono	2010-07-23	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	1.75	30	99.6	0.056	27.34	7.1	38224	38224		-3

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)
	1.75	1.78	99		0.565	3.06	6.3	1863

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 (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	THROUGHOUT	3N77	1.75	29.03	36254	36254	1911	99.47	0.18713	0.1855	0.21836	RANDOM	37.45

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]
-2.27			0.19		2.08

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	29.501
r_dihedral_angle_4_deg	12.554
r_dihedral_angle_3_deg	10.538
r_scangle_it	4.046
r_dihedral_angle_1_deg	3.929
r_scbond_it	2.528
r_mcangle_it	1.845
r_angle_refined_deg	1.502
r_mcbond_it	1.017
r_angle_other_deg	0.812

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	29.501
r_dihedral_angle_4_deg	12.554
r_dihedral_angle_3_deg	10.538
r_scangle_it	4.046
r_dihedral_angle_1_deg	3.929
r_scbond_it	2.528
r_mcangle_it	1.845
r_angle_refined_deg	1.502
r_mcbond_it	1.017
r_angle_other_deg	0.812
r_mcbond_other	0.271
r_chiral_restr	0.1
r_bond_refined_d	0.012
r_gen_planes_refined	0.006
r_gen_planes_other	0.002
r_bond_other_d	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2133
Nucleic Acid Atoms
Solvent Atoms	237
Heterogen Atoms	37

Software

Software
Software Name	Purpose
Blu-Ice	data collection
PHASER	phasing
REFMAC	refinement
HKL-3000	data reduction
HKL-3000	data scaling

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.