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 SDS-polyacrylamide gel electrophoresis '''<FONT COLOR="#E42217"> (SDS-PAGE)</FONT>''', high-performance liquid chromatography'''<FONT COLOR="#F535AA"> (HPLC)</FONT>''' 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==