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Expression, purification, crystallization and preliminary X‐ray crystallographic analysis of the SH3 domain of human AHI1

Expression, purification, crystallization and preliminary X‐ray crystallographic analysis of the... The SH3 domain of human AHI1 was cloned and expressed in Escherichia coli. The protein was purified by affinity and size‐exclusion chromatography and was crystallized using the sitting‐drop vapour‐diffusion method at 293 K. A complete data set was collected to 2.5 Å resolution at 110 K. The crystal belonged to space group P41212, with unit‐cell parameters a = 67.377, b = 67.377, c = 98.549 Å. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Expression, purification, crystallization and preliminary X‐ray crystallographic analysis of the SH3 domain of human AHI1

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References (11)

Publisher
Wiley
Copyright
International Union of Crystallography, 2009
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S174430910900774X
pmid
19342780
Publisher site
See Article on Publisher Site

Abstract

The SH3 domain of human AHI1 was cloned and expressed in Escherichia coli. The protein was purified by affinity and size‐exclusion chromatography and was crystallized using the sitting‐drop vapour‐diffusion method at 293 K. A complete data set was collected to 2.5 Å resolution at 110 K. The crystal belonged to space group P41212, with unit‐cell parameters a = 67.377, b = 67.377, c = 98.549 Å.

Journal

Acta Crystallographica Section FWiley

Published: Apr 1, 2009

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