Evidence: scanning transmission electron microscopy, TEM confirms 2D lattice formation of the isolated Sap assembly domain, SAXS, SAXS confirms monomeric state of deposited complex, light scattering, ...Evidence: scanning transmission electron microscopy, TEM confirms 2D lattice formation of the isolated Sap assembly domain, SAXS, SAXS confirms monomeric state of deposited complex, light scattering, DLS show high MW polymer formation of the isolated Sap protein (chain A, B), and stabilization as monomeric unit when in complex with nanobodies NbAF694 and Nb683
Type
Name
Symmetry operation
Number
identity operation
1_555
x,y,z
1
Buried area
10170 Å2
ΔGint
-20 kcal/mol
Surface area
80680 Å2
Method
PISA
Unit cell
Length a, b, c (Å)
74.230, 79.910, 81.230
Angle α, β, γ (deg.)
88.660, 82.000, 85.590
Int Tables number
1
Space group name H-M
P1
-
Components
#1: Protein
S-layerproteinsap / Surface array protein / Surface layer protein
Mass: 64771.430 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: Protein fragment corresponding to the S-layer assembly domain of the B. anthracis surface array protein Sap Source: (gene. exp.) Bacillus anthracis (anthrax bacterium) / Gene: sap, BA_0885, GBAA_0885, BAS0841 / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: P49051
#2: Antibody
NanobodyNbAF683
Mass: 14150.650 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Lama glama (llama) / Production host: Escherichia coli (E. coli) / Strain (production host): WK6
#3: Antibody
NanobodyNbAF694
Mass: 14913.369 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Lama glama (llama) / Production host: Escherichia coli (E. coli) / Strain (production host): WK6
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