Expression, Purification, Crystallization and Preliminary X-Ray Analysis of Human Spindlin1, an Ovarian Cancer-Related Protein

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Abstract:

Human spindlin1 is A newly screened and identified gene product related to ovarian carcinomas and is highly homologous to mouse spindlin. It is an abundant maternal transcript expressed in the mouse during the transition from oocyte to embryo. Here, the recombinant human spindlin1 has been overexpressed in Escherichia coli BL21, purified and crystallized using the hanging-drop vapour-diffusion method. Crystals diffracting to 2.25 Å resolution were obtained using ammonium sulfate as precipitant. The crystals belong to the space group P212121, with unit-cell parameters A =40.7 Å, b =84.4 Å, c =136.4 Å, α=β=γ=90° . Assuming two molecules per asymmetric unit, the solvent content is calculated to be 42.4%.





Keywords: Crystallization; Escherichia coli strain BL21; Y-linked spermiogenesis-specific transcript; c-mos; gametes; tumorigenesis

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986606775101661

Affiliations: Laboratory of Structural Biology, Tsinghua University, Beijing, 100084, China.

Publication date: February 1, 2006

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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