Sandbox Reserved 494: Difference between revisions

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==High resolution structure analysis==

The first atomic-level(2.8Å) resolution structures by '''X-ray''', strucutures was of bovine mitochondrial F1 in 1994. The α and β subunits each had similiar three-domain structure, with an N-terminal β-barrel furthest away from the membrane surface, a central nucleotide-binding domain, and a C-terminal helical domain. Also, an '''NMR''' structure of isolated ''E. coli'' ε subunit is in good agreement with X-ray structure. The structure of the N-terminal domain of ''E. coli'' δ subunit consisting of residues 1 through 134 was solved also by NMR <ref name="MM"/>. In addition, according to analyses by ''' SDS-polyacrylamide gel electrophoresis '''(SDS-PAGE) ,''' high-performance liquid chromatography '''(HPLC) analysis, and NH2-terminal sequencing, the purified complex used here for crystallization consists of subunis α, β, γ, δ, ε, b, d, a, h, f, ATP8, and c (in diminishing apparent molecular weight order for F1 and F0 on SDS gels) and is similar to other preparations.

The first atomic-level (2.8Å) resolution structures by '''X-ray''', strucutures was of bovine mitochondrial F1 in 1994. The α and β subunits each had similiar three-domain structure, with an N-terminal β-barrel furthest away from the membrane surface, a central nucleotide-binding domain, and a C-terminal helical domain. Also, an '''NMR''' structure of isolated ''E. coli'' ε subunit is in good agreement with X-ray structure. The structure of the N-terminal domain of ''E. coli'' δ subunit consisting of residues 1 through 134 was solved also by NMR <ref name="MM"/>. In addition, according to analyses by ''' SDS-polyacrylamide gel electrophoresis '''(SDS-PAGE) ,''' high-performance liquid chromatography '''(HPLC) analysis, and NH2-terminal sequencing, the purified complex used here for crystallization consists of subunis α, β, γ, δ, ε, b, d, a, h, f, ATP8, and c (in diminishing apparent molecular weight order for F1 and F0 on SDS gels) and is similar to other preparations.

==Reaction analysis of the catalytic sites==

Sandbox Reserved 494: Difference between revisions

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 ==High resolution structure analysis==
-The first atomic-level(2.8Å) resolution structures by '''<FONT COLOR="#F87217">X-ray</FONT>''', strucutures was of bovine mitochondrial F<sub>1</sub> in 1994. The α and β subunits each had similiar three-domain structure, with an N-terminal β-barrel furthest away from the membrane surface, a central nucleotide-binding domain, and a C-terminal helical domain. Also, an '''<FONT COLOR="#571B7e">NMR</FONT>''' structure of isolated ''E. coli'' ε subunit is in good agreement with X-ray structure. The structure of the N-terminal domain of ''E. coli'' δ subunit consisting of residues 1 through 134 was solved also by NMR <ref name="MM"/>. In addition, according to analyses by '''<FONT COLOR="#E42217"> SDS-polyacrylamide gel electrophoresis </FONT>'''(SDS-PAGE) ,'''<FONT COLOR="#F535AA"> high-performance liquid chromatography </FONT>'''(HPLC) analysis, and NH<sub>2</sub>-terminal sequencing, the purified complex used here for crystallization consists of subunis α, β, γ, δ, ε, b, d, a, h, f, ATP8, and c (in diminishing apparent molecular weight order for F<sub>1</sub> and F<sub>0</sub> on SDS gels) and is similar to other preparations.
+The first atomic-level (2.8Å) resolution structures by '''<FONT COLOR="#F87217">X-ray</FONT>''', strucutures was of bovine mitochondrial F<sub>1</sub> in 1994. The α and β subunits each had similiar three-domain structure, with an N-terminal β-barrel furthest away from the membrane surface, a central nucleotide-binding domain, and a C-terminal helical domain. Also, an '''<FONT COLOR="#571B7e">NMR</FONT>''' structure of isolated ''E. coli'' ε subunit is in good agreement with X-ray structure. The structure of the N-terminal domain of ''E. coli'' δ subunit consisting of residues 1 through 134 was solved also by NMR <ref name="MM"/>. In addition, according to analyses by '''<FONT COLOR="#E42217"> SDS-polyacrylamide gel electrophoresis </FONT>'''(SDS-PAGE) ,'''<FONT COLOR="#F535AA"> high-performance liquid chromatography </FONT>'''(HPLC) analysis, and NH<sub>2</sub>-terminal sequencing, the purified complex used here for crystallization consists of subunis α, β, γ, δ, ε, b, d, a, h, f, ATP8, and c (in diminishing apparent molecular weight order for F<sub>1</sub> and F<sub>0</sub> on SDS gels) and is similar to other preparations.
 ==Reaction analysis of the catalytic sites==