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Crystallization and preliminary X‐ray analysis of tyrosine aminotransferase from Trypanosoma cruziepimastigotes
- Source :
- Acta Crystallographica Section D: Biological Crystallography; November 1998, Vol. 54 Issue: 1 p105-107, 3p
- Publication Year :
- 1998
-
Abstract
- Tyrosine aminotransferase from Trypanosoma cruzihas been crystallized from PEG 4000 at pH 6.8. The crystals belong to the monoclinic space group P21and have lattice constants of a= 59.1, b= 103.0, c= 77.8 Å, β = 113.1° for a data set measured at 138 K. The presence of a non‐crystallographic twofold axis together with a Matthews parameter Vmof 2.5 Å3Da−1indicates that the asymmetric unit contains one dimeric molecule. The crystals diffract to at least 2.7 Å and are stable in the X‐ray beam in a shock‐frozen state. Native data sets have been collected at temperatures of 285 and 138 K using a Siemens X1000 detector on a rotating‐anode generator.
Details
- Language :
- English
- ISSN :
- 09074449 and 13990047
- Volume :
- 54
- Issue :
- 1
- Database :
- Supplemental Index
- Journal :
- Acta Crystallographica Section D: Biological Crystallography
- Publication Type :
- Periodical
- Accession number :
- ejs24255046
- Full Text :
- https://doi.org/10.1107/S0907444997008019