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PDBsum entry 2fk5
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References listed in PDB file
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Key reference
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Title
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Purification, Crystallization and preliminary X-Ray crystallographic study of the l-Fuculose-1-Phosphate aldolase (fuca) from thermus thermophilus hb8.
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Authors
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J.Jeyakanthan,
J.Taka,
A.Kikuchi,
C.Kuroishi,
K.Yutani,
Y.Shiro.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2005,
61,
1075-1077.
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PubMed id
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Abstract
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Fuculose phosphate aldolase catalyzes the reversible cleavage of
L-fuculose-1-phosphate to dihydroxyacetone phosphate and L-lactaldehyde. The
protein from Thermus thermophilus HB8 is a biological tetramer with a subunit
molecular weight of 21 591 Da. Purified FucA has been crystallized using
sitting-drop vapour-diffusion and microbatch techniques at 293 K. The crystals
belong to space group P4, with unit-cell parameters a = b = 100.94, c = 45.87 A.
The presence of a dimer of the enzyme in the asymmetric unit was estimated to
give a Matthews coefficient (VM) of 2.7 A3 Da(-1) and a solvent content of
54.2%(v/v). Three-wavelength diffraction MAD data were collected to 2.3 A from
zinc-containing crystals. Native diffraction data to 1.9 A resolution have been
collected using synchrotron radiation at SPring-8.
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