TY - JOUR
T1 - Crystallization of halophilic malate dehydrogenase from Halobacterium marismortui
AU - Harel, M.
AU - Shoham, M.
AU - Frolow, F.
AU - Eisenberg, H.
AU - Mevarech, M.
AU - Yonath, A.
AU - Sussman, J. L.
N1 - Funding Information:
This work was supportedi n part by a grant from the
PY - 1988/4/5
Y1 - 1988/4/5
N2 - Malate dehydrogenase from the extreme halophile Halobacterium marismortui crystallizes in highly concentrated phosphate solution in space group I2 with cell dimensions a = 113.8 A ̊, b = 122.8 A ̊, c = 126.7 A ̊, β = 98.1 °. The halophilic enzyme was found to be unstable at lower concentrations of phosphate. It associates with unusually large amounts of water and salt, and the combined particle volume shows a tight fit in the unit cell.
AB - Malate dehydrogenase from the extreme halophile Halobacterium marismortui crystallizes in highly concentrated phosphate solution in space group I2 with cell dimensions a = 113.8 A ̊, b = 122.8 A ̊, c = 126.7 A ̊, β = 98.1 °. The halophilic enzyme was found to be unstable at lower concentrations of phosphate. It associates with unusually large amounts of water and salt, and the combined particle volume shows a tight fit in the unit cell.
UR - http://www.scopus.com/inward/record.url?scp=0024278428&partnerID=8YFLogxK
U2 - 10.1016/0022-2836(88)90547-5
DO - 10.1016/0022-2836(88)90547-5
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AN - SCOPUS:0024278428
SN - 0022-2836
VL - 200
SP - 609
EP - 610
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 3
ER -