4RQA

Crystal Structure of a Hypoxanthine Phosphoribosyltransferase (target ID NYSGRC-029686) from Staphylococcus aureus (orthorhombic space group)

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	4.6	293	0.1 M Sodium Acetate, 3.5 M Sodium Formate, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K

Crystal Properties
Matthews coefficient	Solvent content
2.89	57.37

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 66.158	α = 90
b = 71.919	β = 90
c = 103.036	γ = 90

Symmetry
Space Group	I 2 2 2

Diffraction

Diffraction Experiment
ID #	Crystal ID	Scattering Type	Data Collection Temperature	Detector	Detector Type	Details	Collection Date	Monochromator	Protocol
1	1	x-ray	77	CCD	ADSC QUANTUM 315	MIRRORS	2013-07-19	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	NSLS BEAMLINE X29A	0.9790, 1.075	NSLS	X29A

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	1.48	20	98.3	0.073	14.8	7.8	41368	40663

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	1.48	1.51	100		0.94		7.6	2035

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	1.48	20	41362	40663	2038	98.05	0.1519	0.1497	0.1942	RANDOM	32.072

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]
-0.48			0.18		0.3

RMS Deviations
Key	Refinement Restraint Deviation
r_sphericity_free	37.637
r_dihedral_angle_2_deg	29.708
r_sphericity_bonded	24.596
r_dihedral_angle_4_deg	17.48
r_dihedral_angle_3_deg	14.279
r_mcangle_it	11.624
r_mcbond_it	9.874
r_mcbond_other	9.746
r_rigid_bond_restr	6.953
r_dihedral_angle_1_deg	6.253

RMS Deviations
Key	Refinement Restraint Deviation
r_sphericity_free	37.637
r_dihedral_angle_2_deg	29.708
r_sphericity_bonded	24.596
r_dihedral_angle_4_deg	17.48
r_dihedral_angle_3_deg	14.279
r_mcangle_it	11.624
r_mcbond_it	9.874
r_mcbond_other	9.746
r_rigid_bond_restr	6.953
r_dihedral_angle_1_deg	6.253
r_angle_refined_deg	2.344
r_angle_other_deg	1.56
r_chiral_restr	0.132
r_bond_refined_d	0.025
r_gen_planes_refined	0.014
r_gen_planes_other	0.009
r_bond_other_d	0.002

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1394
Nucleic Acid Atoms
Solvent Atoms	113
Heterogen Atoms	20

Software

Software
Software Name	Purpose
DENZO	data reduction
SCALEPACK	data scaling
REFMAC	refinement
PDB_EXTRACT	data extraction
CBASS	data collection
HKL-3000	data reduction
HKL2Map	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.