Document Detail

Purification, crystallization and preliminary crystallographic analysis of a thermostable endonuclease IV from Thermotoga maritima.
MedLine Citation:
PMID:  20054139     Owner:  NLM     Status:  MEDLINE    
The DNA-repair enzyme endonuclease IV from the thermophilic bacterium Thermotoga maritima MSB8 (reference sequence NC_000853) has been expressed in Escherichia coli and crystallized for X-ray analysis. T. maritima endonuclease IV is a 287-amino-acid protein with 32% sequence identity to E. coli endonuclease IV. The protein was purified to homogeneity and was crystallized using the sitting-drop vapor-diffusion method. The protein crystallized in space group P6(1), with one biological molecule in the asymmetric unit, corresponding to a Matthews coefficient of 2.39 A(3) Da(-1) and 47% solvent content. The unit-cell parameters of the crystals were a = b = 123.2, c = 35.6 A. Microseeding and further optimization yielded crystals with an X-ray diffraction limit of 2.36 A. A single 70 degrees data set was collected and processed, resulting in an overall R(merge) and a completeness of 9.5% and 99.3%, respectively.
Ronny C Hughes; Stephen J Tomanicek; Joseph D Ng; Leighton Coates
Related Documents :
15299619 - Crystallization and preliminary x-ray analysis of a bifunctional enzyme: hhdd isomerase...
21577519 - (e)-3-dimethyl-amino-1-(4-pyrid-yl)prop-2-en-1-one.
17196979 - Reversible inhibition of escherichia coli inorganic pyrophosphatase by fluoride: trappe...
8639589 - Domain closure in adenylate kinase.
15929999 - X-ray structure of putative acyl-acp desaturase desa2 from mycobacterium tuberculosis h...
8980119 - Isolation, crystallization and x-ray analysis of the quaternary complex of phe-trna(phe...
24588569 - Octakis(tert-butoxo)dicerium(iv) [ce2(o(t)bu)8]: synthesis, characterization, decomposi...
19201439 - Removal of arsenic from water: effect of calcium ions on as(iii) removal in the kmno(4)...
15525199 - Robust dx2-y2 pairing symmetry in hole-doped cuprate superconductors.
Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2009-11-27
Journal Detail:
Title:  Acta crystallographica. Section F, Structural biology and crystallization communications     Volume:  65     ISSN:  1744-3091     ISO Abbreviation:  Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.     Publication Date:  2009 Dec 
Date Detail:
Created Date:  2010-01-07     Completed Date:  2010-03-19     Revised Date:  2013-05-31    
Medline Journal Info:
Nlm Unique ID:  101226117     Medline TA:  Acta Crystallogr Sect F Struct Biol Cryst Commun     Country:  England    
Other Details:
Languages:  eng     Pagination:  1317-9     Citation Subset:  IM    
Oak Ridge National Laboratory, Neutron Scattering Science Division, 1 Bethel Valley Road, Oak Ridge, TN 37831, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Crystallography, X-Ray
Deoxyribonuclease IV (Phage T4-Induced) / chemistry*,  genetics,  isolation & purification
Enzyme Stability
Recombinant Proteins / chemistry,  genetics,  isolation & purification
Thermotoga maritima / enzymology*,  genetics
Reg. No./Substance:
0/Recombinant Proteins; EC IV (Phage T4-Induced)

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Expression, purification, crystallization and preliminary X-ray analysis of maleylacetate reductase ...
Next Document:  Lamellar body exocytosis by cell stretch or purinergic stimulation: possible physiological roles, me...