Crystallization and preliminary X‐ray analysis of the CRP–cAMP–DNA (full length) complex. Issue 5 (22nd May 2013)

• Record Type: Journal Article
• Authors: Huang, Jing; Liu, Jing; Tao, Wenbing; Yang, Zhenxing; Qiu, Rui; Yu, Shaoning; Ji, Chaoneng
• Is Part Of: Acta crystallographica. Volume 69:Issue 5(2013:May)
• Page Start: 562
• Page End: 565
• Publication Date: 2013-05-22
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113009925
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The <italic>Escherichia coli</italic> cyclic AMP receptor protein (CRP) is a well known transcription activator protein. In this study, CRP was overexpressed, purified and cocrystallized with cAMP and a 38 bp full‐length double‐stranded DNA fragment. The full‐length segment differed from the half‐site fragments used in previous crystallization experiments and is more similar to the environment <italic>in vivo</italic>. CRP–cAMP–DNA crystals were obtained and diffracted to 2.9 Å resolution. The crystals belonged to space group <italic>P</italic>3₁21, with unit‐cell parameters <italic>a</italic> = <italic>b</italic> = 76.03, <italic>c</italic> = 144.00 Å. The asymmetric unit was found to contain one protein molecule and half a 38 bp full‐length double‐stranded DNA fragment, with a Matthews coefficient of 2.62 ų Da⁻¹ and a solvent content of 53.14%.</p> </abstract>