3C0F

Crystal Structure of a novel non-Pfam protein AF1514 from Archeoglobus fulgidus DSM 4304 solved by S-SAD using a Cr X-ray source

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	5	291	0.1 M sodium chloride, 0.1 M sodium acetate trihydrate, 10 % v/v MPD, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K

Crystal Properties
Matthews coefficient	Solvent content
3.09	60.19

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 49.737	α = 90
b = 49.737	β = 90
c = 106.462	γ = 90

Symmetry
Space Group	P 41 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	IMAGE PLATE	RIGAKU RAXIS IV++		2007-11-12	M	SINGLE WAVELENGTH
2	1		IMAGE PLATE	RIGAKU RAXIS IV++		2007-11-18

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	ROTATING ANODE	RIGAKU FR-E+ SUPERBRIGHT
2	ROTATING ANODE	RIGAKU MICROMAX-007	2.29

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	R Sym 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	1.8	45.08	91.4	0.041	0.042	46.2	9.2	13109	11982	1.7	1.74	26

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	R-Sym I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	1.8	1.86	58		0.215	0.216	4.8	2.5	735

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Resolution (High)	Resolution (Low)	Cut-off Sigma (I)	Cut-off Sigma (F)	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	1.8	45.08	1.8	1.8	13109	11347	575	91.27	0.20652	0.20554	0.22647	RANDOM	19.372

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]
0.65			0.65		-1.31

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	25.942
r_dihedral_angle_4_deg	15.08
r_dihedral_angle_3_deg	10.344
r_dihedral_angle_1_deg	5.217
r_scangle_it	1.058
r_angle_refined_deg	1.009
r_scbond_it	0.698
r_mcangle_it	0.49
r_nbtor_refined	0.307
r_mcbond_it	0.28

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	25.942
r_dihedral_angle_4_deg	15.08
r_dihedral_angle_3_deg	10.344
r_dihedral_angle_1_deg	5.217
r_scangle_it	1.058
r_angle_refined_deg	1.009
r_scbond_it	0.698
r_mcangle_it	0.49
r_nbtor_refined	0.307
r_mcbond_it	0.28
r_nbd_refined	0.171
r_symmetry_vdw_refined	0.158
r_symmetry_hbond_refined	0.073
r_xyhbond_nbd_refined	0.064
r_chiral_restr	0.058
r_bond_refined_d	0.007
r_gen_planes_refined	0.003

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	682
Nucleic Acid Atoms
Solvent Atoms	121
Heterogen Atoms

Software

Software
Software Name	Purpose
REFMAC	refinement
HKL-2000	data collection
HKL-2000	data reduction
HKL-2000	data scaling
SHARP	phasing

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.