3C8V

Crystal structure of putative acetyltransferase (YP_390128.1) from Desulfovibrio desulfuricans G20 at 2.28 A resolution

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	7.3	277	NANODROP, 0.2M K Formate, 20.0% PEG 3350, No Buffer pH 7.3, VAPOR DIFFUSION, SITTING DROP, temperature 277K

Crystal Properties
Matthews coefficient	Solvent content
2.82	56.34

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 249.617	α = 90
b = 249.617	β = 90
c = 104.9	γ = 120

Symmetry
Space Group	H 3

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		2007-09-15	M	MAD

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	ALS BEAMLINE 8.2.1	1.0000, 0.9795, 0.9797	ALS	8.2.1

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	2.28	48.057	94.6	0.054	13.25	2.75		105055		-3	41.55

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	2.28	2.36	67.6		0.446	2.1	2.09

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	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	MAD	THROUGHOUT	2.28	48.057	105052	5271	95.14	0.182	0.18	0.223	RANDOM	40.479

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]
-0.86	-0.43		-0.86		1.3

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	33.297
r_dihedral_angle_4_deg	20.225
r_dihedral_angle_3_deg	15.725
r_dihedral_angle_1_deg	6.633
r_scangle_it	6.434
r_scbond_it	4.305
r_mcangle_it	2.386
r_angle_other_deg	1.571
r_angle_refined_deg	1.478
r_mcbond_it	1.262

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	33.297
r_dihedral_angle_4_deg	20.225
r_dihedral_angle_3_deg	15.725
r_dihedral_angle_1_deg	6.633
r_scangle_it	6.434
r_scbond_it	4.305
r_mcangle_it	2.386
r_angle_other_deg	1.571
r_angle_refined_deg	1.478
r_mcbond_it	1.262
r_mcbond_other	0.435
r_chiral_restr	0.074
r_bond_refined_d	0.013
r_gen_planes_refined	0.006
r_gen_planes_other	0.003
r_bond_other_d	0.002

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	14264
Nucleic Acid Atoms
Solvent Atoms	540
Heterogen Atoms	125

Software

Software
Software Name	Purpose
REFMAC	refinement
PHENIX	refinement
SHELX	phasing
MolProbity	model building
XSCALE	data scaling
PDB_EXTRACT	data extraction
ADSC	data collection
XDS	data reduction
SHELXD	phasing
autoSHARP	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.