1b8z

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(New page: 200px<br /><applet load="1b8z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b8z, resolution 1.6&Aring;" /> '''HU FROM THERMOTOGA MA...)
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[[Image:1b8z.jpg|left|200px]]<br /><applet load="1b8z" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1b8z.jpg|left|200px]]<br /><applet load="1b8z" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1b8z, resolution 1.6&Aring;" />
caption="1b8z, resolution 1.6&Aring;" />
'''HU FROM THERMOTOGA MARITIMA'''<br />
'''HU FROM THERMOTOGA MARITIMA'''<br />
==Overview==
==Overview==
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The humar gene encoding for the histone-like DNA-binding protein HU from, the hyperthermophilic eubacterium Thermotoga maritima was efficiently, overexpressed in Escherichia coli under the T7 promoter. The HU protein, was purified using SP-Sepharose ion-exchange and heparin-affinity, chromatography and was successfully crystallized in ammonium sulfate. The, crystals were grown in the tetragonal form in space group P43 or P41 and, have unit-cell dimensions a = b = 46.12, c = 77.56 A, alpha = beta = gamma, = 90 degrees. The crystals diffract X-rays to 1.6 A resolution using, synchrotron radiation and are suitable for determination of the HU, structure at high resolution.
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The humar gene encoding for the histone-like DNA-binding protein HU from the hyperthermophilic eubacterium Thermotoga maritima was efficiently overexpressed in Escherichia coli under the T7 promoter. The HU protein was purified using SP-Sepharose ion-exchange and heparin-affinity chromatography and was successfully crystallized in ammonium sulfate. The crystals were grown in the tetragonal form in space group P43 or P41 and have unit-cell dimensions a = b = 46.12, c = 77.56 A, alpha = beta = gamma = 90 degrees. The crystals diffract X-rays to 1.6 A resolution using synchrotron radiation and are suitable for determination of the HU structure at high resolution.
==About this Structure==
==About this Structure==
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1B8Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B8Z OCA].
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1B8Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B8Z OCA].
==Reference==
==Reference==
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[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Christodoulou, E.]]
[[Category: Christodoulou, E.]]
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[[Category: Rypniewski, W.R.]]
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[[Category: Rypniewski, W R.]]
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[[Category: Vorgias, C.E.]]
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[[Category: Vorgias, C E.]]
[[Category: thermostable dna binding protein]]
[[Category: thermostable dna binding protein]]
[[Category: thermotoga maritima]]
[[Category: thermotoga maritima]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:28:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:52:52 2008''

Revision as of 09:52, 21 February 2008


1b8z, resolution 1.6Å

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HU FROM THERMOTOGA MARITIMA

Overview

The humar gene encoding for the histone-like DNA-binding protein HU from the hyperthermophilic eubacterium Thermotoga maritima was efficiently overexpressed in Escherichia coli under the T7 promoter. The HU protein was purified using SP-Sepharose ion-exchange and heparin-affinity chromatography and was successfully crystallized in ammonium sulfate. The crystals were grown in the tetragonal form in space group P43 or P41 and have unit-cell dimensions a = b = 46.12, c = 77.56 A, alpha = beta = gamma = 90 degrees. The crystals diffract X-rays to 1.6 A resolution using synchrotron radiation and are suitable for determination of the HU structure at high resolution.

About this Structure

1B8Z is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

Cloning, overproduction, purification and crystallization of the DNA binding protein HU from the hyperthermophilic eubacterium Thermotoga maritima., Christodoulou E, Vorgias CE, Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):1043-5. PMID:9757133

Page seeded by OCA on Thu Feb 21 11:52:52 2008

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