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NTIS 바로가기Acta crystallographica. Section D, Biological crystallography, v.71 no.3, 2015년, pp.541 - 554
Arai, Shigeki (Quantum Beam Science Directorate, Japan Atomic Energy Agency , 2-4 Shirakata-shirane, Tokai, Ibaraki 319-1195, Japan) , Yonezawa, Yasushi (Quantum Beam Science Directorate, Japan Atomic Energy Agency , 2-4 Shirakata-shirane, Tokai, Ibaraki 319-1195, Japan) , Okazaki, Nobuo (Quantum Beam Science Directorate, Japan Atomic Energy Agency , 2-4 Shirakata-shirane, Tokai, Ibaraki 319-1195, Japan) , Matsumoto, Fumiko (Quantum Beam Science Directorate, Japan Atomic Energy Agency , 2-4 Shirakata-shirane, Tokai, Ibaraki 319-1195, Japan) , Shibazaki, Chie (Quantum Beam Science Directorate, Japan Atomic Energy Agency , 2-4 Shirakata-shirane, Tokai, Ibaraki 319-1195, Japan) , Shimizu, Rumi (Quantum Beam Science Directorate, Japan Atomic Energy Agency , 2-4 Shirakata-shirane, Tokai, Ibaraki 319-1195, Japan) , Yamada, Mitsugu (Quantum Beam Science Directorate, Japan Atomic Energy Agency , 2-4 Shirakata-shirane, Tokai, Ibaraki 319-1195, Japan Jap) , Adachi, Motoyasu , Tamada, Taro , Kawamoto, Masahide , Tokunaga, Hiroko , Ishibashi, Matsujiro , Blaber, Michael , Tokunaga, Masao , Kuroki, Ryota
The tertiary structure of a β-lactamase derived from the halobacterium Chromohalobacter sp. 560 (HaBLA) was determined by X-ray crystallography. Three unique Sr2+-binding sites and one Cs+-binding site were discovered in the HaBLA molecule.Environmentally friendly absorbents are needed for Sr2+...
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