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Protein preparation, crystallization and preliminary X-ray analysis of human adrenal gland protein AD-004.
- Source :
- Acta Crystallographica: Section D (Wiley-Blackwell); Jul2004, Vol. 60 Issue 7, p1292-1294, 3p, 1 Black and White Photograph, 1 Diagram, 1 Chart, 1 Graph
- Publication Year :
- 2004
-
Abstract
- The adrenal gland protein AD-004 was identified in the human adrenal gland. Full-length AD-004 contains 172 amino acids, with a predicted molecular weight of about 20 kDa. In attempts to crystallize human AD-004, the gene was subcloned into a modified pET vector, pET21-DEST, with an N-terminal His5 tag using the Gateway cloning system, followed by protein expression in <em>Escherichia coli</em> strain BL21(DE3). The protein was purified in two steps to near-homogeneity and was crystallized. The crystals belong to space group P6<subscript>1</subscript> or P6<subscript>5</subscript>, with unit-cell parameters a = b = 99.56, c = 57.19 Å. A complete 2.0 Å data set has been collected at a rotating-anode X-ray source and structure determination is under way. [ABSTRACT FROM AUTHOR]
- Subjects :
- PROTEINS
ADRENAL glands
AMINO acids
CRYSTALLIZATION
ESCHERICHIA coli
Subjects
Details
- Language :
- English
- ISSN :
- 09074449
- Volume :
- 60
- Issue :
- 7
- Database :
- Complementary Index
- Journal :
- Acta Crystallographica: Section D (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 13877151
- Full Text :
- https://doi.org/10.1107/S0907444904010467