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Purification, crystallization and preliminary X-ray analysis of the fumarylacetoacetase family member TTHA0809 from Thermus thermophilus HB8.

ABSTRACT: Fumarylacetoacetase catalyzes the final step of tyrosine and phenylalanine catabolism. A recombinant form of the fumarylacetoacetase family member TTHA0809 from Thermus thermophilus HB8 has been crystallized by the oil-microbatch method using sodium chloride as a precipitating agent. The crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 93.3, b = 73.4, c = 122.6 A, beta = 111.8 degrees. The crystals are most likely to contain two dimers in the asymmetric unit, with a V(M) value of 3.32 A3 Da(-1). Diffraction data were collected at 2.2 A resolution using synchrotron radiation at beamline BL26B1 of SPring-8, Japan.

SUBMITTER: Mizutani H

PROVIDER: S-EPMC2376325 | biostudies-literature | 2007 Sep

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary X-ray analysis of the fumarylacetoacetase family member TTHA0809 from Thermus thermophilus HB8.

Mizutani Hisashi H Kunishima Naoki N

Acta crystallographica. Section F, Structural biology and crystallization communications 20070831 Pt 9

Fumarylacetoacetase catalyzes the final step of tyrosine and phenylalanine catabolism. A recombinant form of the fumarylacetoacetase family member TTHA0809 from Thermus thermophilus HB8 has been crystallized by the oil-microbatch method using sodium chloride as a precipitating agent. The crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 93.3, b = 73.4, c = 122.6 A, beta = 111.8 degrees. The crystals are most likely to contain two dimers in the asymmetric unit, wi ...[more]

PMID: 17768357

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