1tec: Difference between revisions

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[[Image:1tec.jpg|left|200px]]
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[[Image:1tec.png|left|200px]]


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{{STRUCTURE_1tec|  PDB=1tec  |  SCENE=  }}  
{{STRUCTURE_1tec|  PDB=1tec  |  SCENE=  }}  


'''CRYSTALLOGRAPHIC REFINEMENT BY INCORPORATION OF MOLECULAR DYNAMICS. THE THERMOSTABLE SERINE PROTEASE THERMITASE COMPLEXED WITH EGLIN-C'''
===CRYSTALLOGRAPHIC REFINEMENT BY INCORPORATION OF MOLECULAR DYNAMICS. THE THERMOSTABLE SERINE PROTEASE THERMITASE COMPLEXED WITH EGLIN-C===




==Overview==
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In order to investigate the principles of protein thermostability, the crystal structure of thermitase from Thermoactinomyces vulgaris, a thermostable member of the subtilisin family of serine proteases, has been determined in a complex with eglin c. Eglin c is a serine protease inhibitor from the leech Hirudo medicinalis. After data collection with a television area-detector diffractometer and initial structure solution by molecular-replacement methods, crystallographic refinement proceeded with incorporation of molecular-dynamics techniques. It appeared that this refinement procedure has a large convergence radius with movements of more than 5 A for many atoms. Two procedures for the crystallographic molecular-dynamics refinement have been tested. They differed mainly in time span and weight on the X-ray 'energy'. The best results were obtained with a procedure which allowed the molecular-dynamics technique to search a large area in conformational space by having less weight on the X-ray restraints and allowing more time. The use of molecular-dynamics refinement considerably simplified the laborious and difficult task of fitting the model in its electron density during the refinement process. The final crystallographic R factor is 17.9% at 2.2 A resolution.
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{{ABSTRACT_PUBMED_2688688}}


==About this Structure==
==About this Structure==
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[[Category: Gros, P.]]
[[Category: Gros, P.]]
[[Category: Hol, W G.J.]]
[[Category: Hol, W G.J.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 09:50:57 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:05:31 2008''

Revision as of 14:05, 27 July 2008

File:1tec.png

Template:STRUCTURE 1tec

CRYSTALLOGRAPHIC REFINEMENT BY INCORPORATION OF MOLECULAR DYNAMICS. THE THERMOSTABLE SERINE PROTEASE THERMITASE COMPLEXED WITH EGLIN-C

Template:ABSTRACT PUBMED 2688688

About this Structure

1TEC is a Protein complex structure of sequences from Hirudo medicinalis and Thermoactinomyces vulgaris. Full crystallographic information is available from OCA.

Reference

Crystallographic refinement by incorporation of molecular dynamics: thermostable serine protease thermitase complexed with eglin c., Gros P, Fujinaga M, Dijkstra BW, Kalk KH, Hol WG, Acta Crystallogr B. 1989 Oct 1;45 ( Pt 5):488-99. PMID:2688688

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