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Protein Pept Lett. 2006;13(2):203-5.

Expression, purification, crystallization and preliminary X-ray analysis of human spindlin1, an ovarian cancer-related protein.

Author information

1
Laboratory of Structural Biology, Tsinghua University, Beijing, 100084, China.

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 A resolution were obtained using ammonium sulfate as precipitant. The crystals belong to the space group P2(1)2(1)2(1), with unit-cell parameters a =40.7 A, b =84.4 A, c =136.4 A, alpha=beta=gamma=90 degrees . Assuming two molecules per asymmetric unit, the solvent content is calculated to be 42.4%.

PMID:
16472086
DOI:
10.2174/092986606775101661
[Indexed for MEDLINE]

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