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5
hits found for
Aquifex aeolicus McoA metaloxidase
SASDHL8
–
Aquifex
aeolicus
McoA
metaloxidase
evolved variant (2F4)
Sample:
McoA
evolved variant 2F4 (Periplasmic cell division protein (SufI)) monomer, 55 kDa
Aquifex
aeolicus
VF5
protein
Buffer:
50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment:
SAXS data collected at BM29, ESRF
on 2017 Sep 25
Distal Mutations Shape Substrate-Binding Sites during Evolution of a Metallo-Oxidase into a Laccase
ACS Catalysis
:5022-5035 (2022)
Brissos V, Borges P, Núñez-Franco R, Lucas M, Frazão C, Monza E, Masgrau L, Cordeiro T, Martins L
R
g
Guinier
2.3
nm
D
max
6.8
nm
Volume
Porod
78
nm
3
SASDHM8
–
Aquifex
aeolicus
McoA
metaloxidase
∆328-352 evolved variant (2F4∆328-352)
Sample:
Aquifex
aeolicus
McoA
metaloxidase
∆328-352 evolved variant (2F4∆328-352) monomer, 53 kDa
Aquifex
aeolicus
protein
Buffer:
50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment:
SAXS data collected at BM29, ESRF
on 2018 Jul 18
Distal Mutations Shape Substrate-Binding Sites during Evolution of a Metallo-Oxidase into a Laccase
ACS Catalysis
:5022-5035 (2022)
Brissos V, Borges P, Núñez-Franco R, Lucas M, Frazão C, Monza E, Masgrau L, Cordeiro T, Martins L
R
g
Guinier
2.2
nm
D
max
6.6
nm
Volume
Porod
74
nm
3
SASDFY7
–
Aquifex
aeolicus
McoA
metaloxidase
Sample:
Aquifex
aeolicus
McoA
metaloxidase
monomer, 55 kDa
Aquifex
aeolicus
protein
Buffer:
50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment:
SAXS data collected at B21, Diamond Light Source
on 2019 Apr 15
...
McoA
follows Open-To-Close Transitions with a Role in Enzyme Catalysis
ACS Catalysis
(2020)
Borges P, Brissos V, Hernandez G, Masgrau L, Lucas M, Monza E, Frazão C, Cordeiro T, Martins L
R
g
Guinier
2.3
nm
D
max
7.5
nm
Volume
Porod
79
nm
3
SASDFX7
–
Aquifex
aeolicus
McoA
metaloxidase
deletion mutant ∆337-346 (
MCoA
∆337-346)
Sample:
Aquifex
aeolicus
McoA
metaloxidase
∆337-346 monomer, 54 kDa
Aquifex
aeolicus
protein
Buffer:
50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment:
SAXS data collected at B21, Diamond Light Source
on 2017 Dec 4
...
McoA
follows Open-To-Close Transitions with a Role in Enzyme Catalysis
ACS Catalysis
(2020)
Borges P, Brissos V, Hernandez G, Masgrau L, Lucas M, Monza E, Frazão C, Cordeiro T, Martins L
R
g
Guinier
2.3
nm
D
max
7.0
nm
Volume
Porod
78
nm
3
SASDFW7
–
Aquifex
aeolicus
McoA
metaloxidase
deletion mutant ∆328-352 (
MCoA
∆328-352)
Sample:
Aquifex
aeolicus
McoA
metaloxidase
∆328-352 (
MCoA
∆328-352) monomer, 53 kDa
Aquifex
aeolicus
protein
Buffer:
50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment:
SAXS data collected at BM29, ESRF
on 2017 Jul 13
...
McoA
follows Open-To-Close Transitions with a Role in Enzyme Catalysis
ACS Catalysis
(2020)
Borges P, Brissos V, Hernandez G, Masgrau L, Lucas M, Monza E, Frazão C, Cordeiro T, Martins L
R
g
Guinier
2.3
nm
D
max
6.9
nm
Volume
Porod
77
nm
3