2AZW

Crystal structure of the MutT/nudix family protein from Enterococcus faecalis

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	7.5	298	0.1M HEPES, 25% PEG3350, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K

Crystal Properties
Matthews coefficient	Solvent content
3.19	61

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 90.839	α = 90
b = 90.839	β = 90
c = 52.659	γ = 90

Symmetry
Space Group	P 43 21 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	ADSC QUANTUM 315	mirrors	2005-02-06	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 19-ID	0.9798	APS	19-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	1.9	64.28	99.9	0.086	40.2	9.2	17434	17228	2	2	37

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	1.9	1.97	99.7		0.662	2.7	7.3	3300

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 (All)	R-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	SAD	THROUGHOUT	1.9	64.28	17434	17228	929	98.82	0.19479	0.19479	0.19303	0.22969	RANDOM	36.935

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]
0.58			0.58		-1.15

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	26.646
r_dihedral_angle_3_deg	14.414
r_dihedral_angle_4_deg	14.104
r_dihedral_angle_1_deg	6.554
r_scangle_it	2.408
r_scbond_it	1.589
r_mcangle_it	1.209
r_angle_refined_deg	1.097
r_mcbond_it	0.745
r_nbtor_refined	0.299

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	26.646
r_dihedral_angle_3_deg	14.414
r_dihedral_angle_4_deg	14.104
r_dihedral_angle_1_deg	6.554
r_scangle_it	2.408
r_scbond_it	1.589
r_mcangle_it	1.209
r_angle_refined_deg	1.097
r_mcbond_it	0.745
r_nbtor_refined	0.299
r_nbd_refined	0.185
r_symmetry_vdw_refined	0.179
r_symmetry_hbond_refined	0.174
r_xyhbond_nbd_refined	0.134
r_chiral_restr	0.078
r_bond_refined_d	0.01
r_gen_planes_refined	0.004

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1188
Nucleic Acid Atoms
Solvent Atoms	160
Heterogen Atoms	16

Software

Software
Software Name	Purpose
REFMAC	refinement
SBC-Collect	data collection
HKL-2000	data scaling
CNS	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.