1VLI

Crystal structure of Spore coat polysaccharide biosynthesis protein spsE (BSU37870) from Bacillus subtilis at 2.38 A resolution

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION,SITTING DROP,NANODROP		277	18% PEG MME 2000, 0.04M Tris_base, 0.06M Tris Cl , VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 277K

Crystal Properties
Matthews coefficient	Solvent content
3.74	66.82

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 70.578	α = 90
b = 70.578	β = 90
c = 205.359	γ = 120

Symmetry
Space Group	P 32 2 1

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	ADSC Flat mirror	2004-05-20	M	SINGLE WAVELENGTH
2	1	x-ray		M	MAD
1,2	1

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	SSRL BEAMLINE BL9-1		SSRL	BL9-1
2	SYNCHROTRON	SSRL BEAMLINE BL9-1	0.879288, 0.978780, 0.979359	SSRL	BL9-1

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (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
1,2	2.38	29.29	99.9	0.076	13.5	6.9		24673			61.62

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R-Sym I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1,2	2.38	2.51	99.6		0.7	2.3	5.9	3515

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	2.38	29.29	23362	1256	99.82	0.19271	0.19035	0.23799	RANDOM	62.978

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]
-3.57	-1.78		-3.57		5.35

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	40.701
r_dihedral_angle_3_deg	16.513
r_dihedral_angle_4_deg	15.146
r_scangle_it	8.737
r_dihedral_angle_1_deg	6.475
r_scbond_it	6.435
r_mcangle_it	3.719
r_mcbond_it	2.225
r_angle_refined_deg	1.508
r_nbtor_refined	0.308

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	40.701
r_dihedral_angle_3_deg	16.513
r_dihedral_angle_4_deg	15.146
r_scangle_it	8.737
r_dihedral_angle_1_deg	6.475
r_scbond_it	6.435
r_mcangle_it	3.719
r_mcbond_it	2.225
r_angle_refined_deg	1.508
r_nbtor_refined	0.308
r_nbd_refined	0.208
r_symmetry_hbond_refined	0.172
r_xyhbond_nbd_refined	0.129
r_symmetry_vdw_refined	0.119
r_chiral_restr	0.114
r_bond_refined_d	0.017
r_gen_planes_refined	0.005

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2739
Nucleic Acid Atoms
Solvent Atoms	83
Heterogen Atoms	1

Software

Software
Software Name	Purpose
XDSauto	data collection
SCALA	data scaling
SHARP	phasing
autoSHARP	phasing
SOLOMON	phasing
REFMAC	refinement
XDS	data reduction
CCP4	data scaling

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.