Crystallization and preliminary X-ray diffraction analysis of the extracellular domain of the cell surface antigen CD38 complexed with ganglioside.

Crystallization and preliminary X-ray diffraction analysis of the extracellular domain of the cell surface antigen CD38 complexed with ganglioside. Research Abstract Details 

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Crystallization and preliminary X-ray diffraction analysis of the extracellular domain of the cell surface antigen CD38 complexed with ganglioside. Abstract Text:

M Kukimoto,O Nureki,M Shirouzu,T Katada,Y Hirabayashi,H Sugiya,S Furuyama,S Yokoyama,M Hara-Yokoyama,

The cell surface antigen CD38 is a multifunctional ectoenzyme that acts as an NAD(+) glycohydrolase, an ADP-ribosyl cyclase, and also a cyclic ADP-ribose hydrolase. The extracellular catalytic domain of CD38 was expressed as a fusion protein with maltose-binding protein, and was crystallized in the complex with a ganglioside, G(T1b), one of the possible physiological inhibitors of this ectoenzyme. Two different crystal forms were obtained using the hanging-drop vapor diffusion method with PEG 10,000 as the precipitant. One form diffracted up to 2.4 A resolution with synchrotron radiation at 100 K, but suffered serious X-ray damage. It belongs to the space group P2(1)2(1)2(1) with unit-cell parameters of a = 47.9, b = 94.9, c = 125.2 A. The other form is a thin plate, but the data sets were successfully collected up to 2.4 A resolution by use of synchrotron radiation at 100 K. The crystals belong to the space group P2(1) with unit-cell parameters of a = 57.4, b = 51.2, c = 101.1 A, and beta = 97.9 degrees, and contain one molecule per asymmetric unit with a VM value of 2.05 A(3)/Da.

Crystallization and preliminary X-ray diffraction analysis of the extracellular domain of the cell surface antigen CD38 complexed with ganglioside. Publishing Authors By Initials

M Kukimoto,O Nureki,M Shirouzu,T Katada,Y Hirabayashi,H Sugiya,S Furuyama,S Yokoyama,M Hara-Yokoyama,

For similar investigative techniques: chemistry, analytical: crystallography: x-ray diffraction research abstracts see: investigative techniques: chemistry, analytical: crystallography: x-ray diffraction research

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Crystallization and preliminary X-ray diffraction analysis of the extracellular domain of the cell surface antigen CD38 complexed with ganglioside. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 127

Page Numbers: 181-4

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Feb

YEAR: 2000

Crystallization and preliminary X-ray diffraction analysis of the extracellular domain of the cell surface antigen CD38 complexed with ganglioside. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Crystallization and preliminary X-ray diffraction analysis of the extracellular domain of the cell surface antigen CD38 complexed with ganglioside. Keywords Mesh Terms:

KEYWORDS: X-Ray Diffraction

MESH TERMS: metabolism

Chemical & Substance for Abstract: Crystallization and preliminary X-ray diffraction analysis of the extracellular domain of the cell surface antigen CD38 complexed with ganglioside. Information

Substance Name: NAD+ Nucleosidase

Registry Number: EC 3.2.2.5

Grant and Affiliation Information for Crystallization and preliminary X-ray diffraction analysis of the extracellular domain of the cell surface antigen CD38 complexed with ganglioside.

AFFILIATION: Cellular Signaling Laboratory, Frontier Research Program, RIKEN (The Institute of Physical and Chemical Research), Hirosawa, Wako-shi, Saitama, 351-0198, Japan.

Country: JAPAN

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MEDLINETA: J Biochem

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