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Crystallization and preliminary X-ray diffraction analysis of the S-adenosylhomocysteine hydrolase (SAHH) from Thermotoga maritima.
- Source :
- Acta Crystallographica: Section F, Structural Biology Communications; Nov2014, Vol. 70 Issue 11, p1563-1565, 3p
- Publication Year :
- 2014
-
Abstract
- S-Adenosylhomocysteine hydrolase (SAHH) catalyzes the reversible conversion of S-adenosylhomocysteine into adenosine and homocysteine. The SAHH from Thermotoga maritima ( TmSAHH) was expressed in Escherichia coli and the recombinant protein was purified and crystallized. TmSAHH crystals belonging to space group C2, with unit-cell parameters a = 106.3, b = 112.0, c = 164.9 Å, β = 103.5°, were obtained by the sitting-drop vapour-diffusion method and diffracted to 2.85 Å resolution. Initial phase determination by molecular replacement clearly indicated that the crystal contains one homotetramer per asymmetric unit. Further refinement of the crystal structure is in progress. [ABSTRACT FROM AUTHOR]
- Subjects :
- HYDROLASES
ADENOSYLHOMOCYSTEINE
ADENOSINES
ESCHERICHIA coli
RECOMBINANT proteins
Subjects
Details
- Language :
- English
- ISSN :
- 2053230X
- Volume :
- 70
- Issue :
- 11
- Database :
- Complementary Index
- Journal :
- Acta Crystallographica: Section F, Structural Biology Communications
- Publication Type :
- Academic Journal
- Accession number :
- 99256030
- Full Text :
- https://doi.org/10.1107/S2053230X14013478