NDLI: Preparation, crystallization and X-ray diffraction analysis to 1.5 A resolution of rat cysteine dioxygenase, a mononuclear iron enzyme responsible for cysteine thiol oxidation.

Please wait, while we are loading the content...

Year: 2013 Volume: 69

Year: 2012 Volume: 68

Year: 2011 Volume: 67

Year: 2010 Volume: 66

Year: 2009 Volume: 65

Year: 2008 Volume: 64

Year: 2007 Volume: 63

Year: 2006 Volume: 62

Year: 2005 Volume: 61

Year: 2005 Volume: 61 Issue: Part 12

Year: 2005 Volume: 61 Issue: Part 11

The ybeY protein from Escherichia coli is a metalloprotein.

Structure of the SARS coronavirus main proteinase as an active C2 crystallographic dimer.

Superoxide reductase from the syphilis spirochete Treponema pallidum: crystallization and structure determination using soft X-rays

Purification, crystallization and preliminary X-ray diffraction analysis of the histone chaperone cia1 from fission yeast.

Cloning, purification, crystallization and preliminary X-ray diffraction analysis of nitrile hydratase from the themophilic Bacillus smithii SC-J05-1.

Expression, purification, crystallization and preliminary crystallographic analysis of human Rad GTPase.

Crystallization and preliminary X-ray diffraction analysis of apolipoprotein E-containing lipoprotein particles.

Overexpression, purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal domain of Ss-LrpB, a transcription regulator from Sulfolobus solfataricus

Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the VP8* carbohydrate-binding protein of the human rotavirus strain Wa.

Crystallization and preliminary X-ray analysis of the isomerase domain of glucosamine-6-phosphate synthase from Candida albicans.

Crystallization and preliminary X-ray diffraction analysis of HML, a lectin from the red marine alga Hypnea musciformis.

Crystallization and preliminary X-ray crystallographic analysis of the Sulfolobus solfataricus nucleotide-exchange factor 1beta.

Overexpression, purification and crystallization of tyrosyl-tRNA synthetase from the hyperthermophilic archaeon Aeropyrum pernix K1

Cloning, purification, crystallization and preliminary crystallographic analysis of a penicillin-binding protein homologue from Pyrococcus abyssi.

Crystallization and preliminary X-ray analysis of the Pax6 paired domain bound to the Pax6 gene enhancer.

Preparation, crystallization and X-ray diffraction analysis to 1.5 A resolution of rat cysteine dioxygenase, a mononuclear iron enzyme responsible for cysteine thiol oxidation.

Crystallization and preliminary X-ray crystallographic studies of fatty acid-CoA racemase from Mycobacterium tuberculosis H37Rv.

Crystallization and preliminary X-ray crystallographic analysis of the GluR0 ligand-binding core from Nostoc punctiforme.

Crystallization and X-ray diffraction properties of Baeyer-Villiger monooxygenase MtmOIV from the mithramycin biosynthetic pathway in Streptomyces argillaceus.

Year: 2005 Volume: 61 Issue: Part 10

Year: 2005 Volume: 61 Issue: Part 9

Year: 2005 Volume: 61 Issue: Part 8

Year: 2005 Volume: 61 Issue: Part 7

Year: 2005 Volume: 61 Issue: Part 6

Year: 2005 Volume: 61 Issue: Part 5

Year: 2005 Volume: 61 Issue: Part 4

Year: 2005 Volume: 61 Issue: Part 3

Year: 2005 Volume: 61 Issue: Part 2

Year: 2005 Volume: 61 Issue: Part 1

Preparation, crystallization and X-ray diffraction analysis to 1.5 A resolution of rat cysteine dioxygenase, a mononuclear iron enzyme responsible for cysteine thiol oxidation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Simmons, Chad R. Hao, Quan Stipanuk, Martha H.
Description	Country affiliation: United States Author Affiliation: Simmons CR ( Division of Nutritional Sciences, Cornell University, Ithaca, NY 14853-8001, USA.)
Abstract	Cysteine dioxygenase (CDO; EC 1.13.11.20) is an approximately 23 kDa non-heme iron metalloenzyme that is responsible for the oxidation of cysteine by O2, yielding cysteinesulfinate. CDO catalyzes the first step in the conversion of cysteine to taurine, as well as the first step in the catabolism of cysteine to pyruvate plus sulfate. Recombinant rat CDO was heterologously expressed, purified and crystallized. The protein was expressed as a fusion protein bearing a polyhistidine tag to facilitate purification, a thioredoxin tag to improve solubility and a factor Xa cleavage site to permit removal of the entire N-terminus, leaving only the 200 amino acids inherent to the native protein. A multi-step purification scheme was used to achieve >95% purity of CDO. The optimal CDO crystals diffracted to 1.5 A resolution and belonged to space group P4(3)2(1)2 or P4(1)2(1)2, with unit-cell parameters a = b = 57.55, c = 123.06 A, alpha = beta = gamma = 90 degrees. CDO shows little homology to any other proteins; therefore, the structure of the enzyme will be determined by ab initio phasing using a selenomethionyl derivative.
File Format	HTM / HTML
ISSN	2053230X
e-ISSN	17443091
Journal	Acta Crystallographica Section F Structural Biology and Crystallization Communications
Issue Number	Pt 11
Volume Number	61
Language	English
Publisher	Wiley
Publisher Date	2005-11-01
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Discipline Crystallography Discipline Biophysics Discipline Molecular Biology Discipline Biochemistry Cysteine Dioxygenase Chemistry Cysteine Sulfhydryl Compounds Animals Binding Sites Catalysis Cloning, Molecular Crystallization Analogs & Derivatives Dna, Complementary Metabolism Dioxygenases Factor Xa Histidine Liver Oxidation-reduction Oxygen Recombinant Fusion Proteins Recombinant Proteins Solubility Temperature X-ray Diffraction Research Support, N.i.h., Extramural Research Support, U.s. Gov't, Non-p.h.s.
Content Type	Text
Resource Type	Article
Subject	Genetics Structural Biology Medicine Biochemistry Biophysics Condensed Matter Physics

Central Library (ISO-9001:2015 Certified)
Indian Institute of Technology Kharagpur
Kharagpur, West Bengal, India | PIN - 721302

See location in the Map
03222 282435
Mail: support@ndl.gov.in

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in