X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase

2002 ◽  
Author(s):  
Misa Kim ◽  
Toshihide Okajima ◽  
Seiichiro Kishishita ◽  
Megumi Yoshimura ◽  
Asako Kawamori ◽  
...  
Keyword(s):  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
X Ray ◽  
Cofactor Biogenesis ◽  
Copper Amine

scholarly journals X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase

2002 ◽  
Vol 58 (s1) ◽  
pp. c298-c298
Author(s):  
M. Kim ◽  
T. Okajima ◽  
S. Kishishita ◽  
M. Yoshimura ◽  
A. Kawamori ◽  
...  
Keyword(s):  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
X Ray ◽  
Cofactor Biogenesis ◽  
Copper Amine

Microcrystal preparation for serial femtosecond X-ray crystallography of bacterial copper amine oxidase

2021 ◽  
Vol 77 (10) ◽  
Author(s):  
Takeshi Murakawa ◽  
Mamoru Suzuki ◽  
Toshi Arima ◽  
Michihiro Sugahara ◽  
Tomoyuki Tanaka ◽  
...  
Keyword(s):  
Free Electron ◽  
Amine Oxidase ◽  
Protein Structures ◽  
Copper Amine Oxidase ◽  
High Quality ◽  
Uniform Size ◽  
Widespread Application ◽  
X Ray ◽  
X Ray Crystallography ◽  
Copper Amine

Recent advances in serial femtosecond X-ray crystallography (SFX) using X-ray free-electron lasers have paved the way for determining radiation-damage-free protein structures under nonfreezing conditions. However, the large-scale preparation of high-quality microcrystals of uniform size is a prerequisite for SFX, and this has been a barrier to its widespread application. Here, a convenient method for preparing high-quality microcrystals of a bacterial quinoprotein enzyme, copper amine oxidase from Arthrobacter globiformis, is reported. The method consists of the mechanical crushing of large crystals (5–15 mm3), seeding the crushed crystals into the enzyme solution and standing for 1 h at an ambient temperature of ∼26°C, leading to the rapid formation of microcrystals with a uniform size of 3–5 µm. The microcrystals diffracted X-rays to a resolution beyond 2.0 Å in SFX measurements at the SPring-8 Angstrom Compact Free Electron Laser facility. The damage-free structure determined at 2.2 Å resolution was essentially identical to that determined previously by cryogenic crystallography using synchrotron X-ray radiation.

Reinvestigation of Metal Ion Specificity for Quinone Cofactor Biogenesis in Bacterial Copper Amine Oxidase†,‡

Biochemistry ◽  
2005 ◽  
Vol 44 (36) ◽  
pp. 12041-12048 ◽  
Author(s):  
Toshihide Okajima ◽  
Sei'ichiro Kishishita ◽  
Yen-Chen Chiu ◽  
Takeshi Murakawa ◽  
Misa Kim ◽  
...  
Keyword(s):  
Metal Ion ◽  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
Ion Specificity ◽  
Cofactor Biogenesis ◽  
Copper Amine

Crystallization and Preliminary X-ray Analysis of Copper Amine Oxidase from Escherichia coli K-12

1994 ◽  
Vol 238 (4) ◽  
pp. 635-637 ◽  
Author(s):  
Jung Hyeob Roh ◽  
Hideyuki Suzuki ◽  
Hidehiko Kumagai ◽  
Mitsuo Yamashita ◽  
Hiroyuki Azakami ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
X Ray ◽  
K 12 ◽  
Copper Amine

scholarly journals Time-resolved analysis of catalytic reaction of copper amine oxidase fromArthrobacter globiformis

2011 ◽  
Vol 67 (a1) ◽  
pp. C225-C225
Author(s):  
H. Yamaguchi ◽  
M. Kataoka ◽  
H. Oya ◽  
A. Tominaga ◽  
M. Ohtsu ◽  
...  
Keyword(s):  
Catalytic Reaction ◽  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
Time Resolved ◽  
Copper Amine
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