| Autor: |
Ito S; Department of Food and Nutritional Sciences, Graduate School of Nutritional and Environmental Sciences, University of Shizuoka, 52-1 Yada, Suruga-Ku, Shizuoka 422-8526, Japan. itosohei@u-shizuoka-ken.ac.jp, Tatsuda E, Ishino K, Suzuki K, Sakai H, Uchida K |
| Jazyk: |
angličtina |
| Zdroj: |
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2006 Jun 01; Vol. 62 (Pt 6), pp. 562-4. Date of Electronic Publication: 2006 May 31. |
| DOI: |
10.1107/S1744309106016630 |
| Abstrakt: |
4-hydroxy-2-nonenal (HNE), a major racemic product of lipid peroxidation, reacts with histidine to form a stable HNE-histidine Michael addition-type adduct possessing three chiral centres in the cyclic hemiacetal structure. Monoclonal antibodies against HNE-modified protein have been widely used for assessing oxidative stress in vitro and in vivo. Here, the purification, crystallization and preliminary crystallographic analysis of a Fab fragment of novel monoclonal antibody R310 (mAbR310), which recognizes (R)-HNE-modified protein, are reported. The Fab fragment of mAbR310 was obtained by digestion with papain, purified and crystallized. Using hanging-drop vapour-diffusion crystallization techniques, crystals of mAbR310 Fab were obtained. The crystal belongs to the monoclinic space group C2 (unit-cell parameters a = 127.04, b = 65.31, c = 64.29 A, beta = 118.88 degrees ) and diffracted X-rays to a resolution of 1.84 A. The asymmetric unit contains one molecule of mAbR310, with a corresponding crystal volume per protein weight of 2.51 A(3) Da(-1) and a solvent content of 51.0%. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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