Crystallization of thermus Thermophilus ICDH
نویسندگان
چکیده
منابع مشابه
Cloning, purification and crystallization of Thermus thermophilus proline dehydrogenase.
Nature recycles L-proline by converting it to L-glutamate. This four-electron oxidation process is catalyzed by the two enzymes: proline dehydrogenase (PRODH) and Delta1-pyrroline-5-carboxylate dehydrogenase. This note reports the cloning, purification and crystallization of Thermus thermophilus PRODH, which is the prototype of a newly discovered superfamily of bacterial monofunctional PRODHs. ...
متن کاملCrystal structure of the 30 S ribosomal subunit from Thermus thermophilus: purification, crystallization and structure determination.
We describe the crystallization and structure determination of the 30 S ribosomal subunit from Thermus thermophilus. Previous reports of crystals that diffracted to 10 A resolution were used as a starting point to improve the quality of the diffraction. Eventually, ideas such as the addition of substrates or factors to eliminate conformational heterogeneity proved less important than attention ...
متن کاملExpression, crystallization and preliminary X-ray analysis of an outer membrane protein from Thermus thermophilus HB27.
The cell envelope of the thermophilic bacterium Thermus thermophilus is multilayered and includes an outer membrane with integral outer membrane proteins that are not well characterized. The hypothetical protein TTC0834 from T. thermophilus HB27 was identified as a 22 kDa outer membrane protein containing eight predicted beta-strands. TTC0834 was expressed with an N-terminal His tag in T. therm...
متن کاملCrystallization and preliminary X-ray analysis of carboxypeptidase 1 from Thermus thermophilus.
Carboxypeptidase 1 from the thermophilic eubacterium Thermus thermophilus (TthCP1, 58 kDa), a member of the M32 family of metallocarboxypeptidases, was crystallized by the sitting-drop vapour-diffusion method using PEG 8000 as the precipitant. The crystals diffracted X-rays to beyond 2.6 A resolution using a synchrotron-radiation source. The crystals belonged to the orthorhombic space group C22...
متن کاملCrystallization and preliminary X-ray crystallographic analysis of peptide deformylase from Thermus thermophilus HB8.
Peptide deformylase (PDF) is responsible for cleaving the formyl group at the N-terminus of nascent polypeptide chains in eubacteria and is essential to bacterial cell viability. A recombinant PDF of the thermophilic bacterium Thermus thermophilus HB8 has been crystallized by the hanging-drop vapour-diffusion method using PEG 4000 as a precipitant. The crystals belonged to the tetragonal space ...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2000
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.40.s158_4