4WVG

Crystal structure of the Type-I signal peptidase from Staphylococcus aureus (SpsB).

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP		296	12 % PEG 8000, 20 % ethylene glycol, 0.2 M amino acids mix (0.2 M sodium-L-glutamate, 0.2 M DL-alanine, 0.2 M glycine, 0.2 M DL-lysine, 0.2 M DL-serine), 100 mM Tris.Cl pH 8.5

Crystal Properties
Matthews coefficient	Solvent content
2.43	49.31

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 57.683	α = 90
b = 63.565	β = 92.59
c = 79.892	γ = 90

Symmetry
Space Group	P 1 21 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 210r		2013-03-25	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	AUSTRALIAN SYNCHROTRON BEAMLINE MX1	0.9537	Australian Synchrotron	MX1

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	Rpim I (All)	CC (Half)	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	2.05	19.44	99.8	0.211	0.082	0.994	10.1	7.6		36318

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	Rpim I (All)	CC (Half)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	2.05	2.11	99.8		1.577	0.608	0.528	1.4	7.6	2779

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	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	MOLECULAR REPLACEMENT	THROUGHOUT	1ANF	2.05	19.44	34468	1839	99.72	0.1921	0.1896	0.242	RANDOM	29.325

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]
-0.72		-0.32	-0.51		1.26

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.687
r_dihedral_angle_3_deg	12.969
r_dihedral_angle_4_deg	8.241
r_dihedral_angle_1_deg	5.331
r_mcangle_it	2.211
r_mcbond_it	1.296
r_mcbond_other	1.296
r_angle_refined_deg	1.16
r_angle_other_deg	0.717
r_chiral_restr	0.066

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.687
r_dihedral_angle_3_deg	12.969
r_dihedral_angle_4_deg	8.241
r_dihedral_angle_1_deg	5.331
r_mcangle_it	2.211
r_mcbond_it	1.296
r_mcbond_other	1.296
r_angle_refined_deg	1.16
r_angle_other_deg	0.717
r_chiral_restr	0.066
r_bond_refined_d	0.007
r_gen_planes_refined	0.004
r_bond_other_d	0.001
r_gen_planes_other	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	3977
Nucleic Acid Atoms
Solvent Atoms	356
Heterogen Atoms	23

Software

Software
Software Name	Purpose
XDS	data scaling
Aimless	data scaling
PHASER	phasing
REFMAC	refinement
PDB_EXTRACT	data extraction

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.