Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus.

Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus. Abstract Text:

Biotin protein ligase from Staphylococcus aureus catalyses the biotinylation of acetyl-CoA carboxylase and pyruvate carboxylase. Recombinant biotin protein ligase from S. aureus has been cloned, expressed and purified. Crystals were grown using the hanging-drop vapour-diffusion method using PEG 8000 as the precipitant at 295 K. X-ray diffraction data were collected to 2.3 A resolution from crystals using synchrotron X-ray radiation at 100 K. The diffraction was consistent with the tetragonal space group P4(2)2(1)2, with unit-cell parameters a = b = 93.665, c = 131.95.

Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus. Publishing Authors By Initials

For similar abstracts research abstracts see: abstracts research

PUBMED ID PMID:

MEDLINE DATE:

Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Acta crystallographica. Section F, Structural biol

VOLUME: 64

Page Numbers: 520-3

Journal Abbreviation: Acta Crystallogr. Sect. F Stru

ISSN: 1744-3091

DAY: 23

MONTH: 05

YEAR: 2008

Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 101226117

Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus. Keywords Mesh Terms:

KEYWORDS:

MESH TERMS:

Chemical & Substance for Abstract: Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus. Information

Substance Name:

Registry Number:

Grant and Affiliation Information for Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus.

AFFILIATION: School of Molecular and Biomedical Sciences, University of Adelaide, North Terrace, Adelaide SA 5005, Australia.

Country: England

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: Acta Crystallogr Sect F Struct

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus Related Publications

• Acetaldehyde-modified proteins and associated antibodies in ethanol-fed rats.
• Alcohol abusers exhibit a higher IgA response to acetaldehyde-modified proteins.
• Cell death and immunohistochemistry of p53, c-Fos and c-Jun after spermine injection into the rat striatum.
• Elevated AP-1 DNA-binding activity in rat brain during ethanol withdrawal.
• Elucidation of a C-rich signature motif in target mRNAs of RNA-binding protein TIAR.
• Generalized no-broadcasting theorem.
• Grb7 SH2 domain structure and interactions with a cyclic peptide inhibitor of cancer cell migration and proliferation.
• Impact of alcohol abuse on protein expression of midkine and excitatory amino acid transporter 1 in the human prefrontal cortex.
• Purification, crystallization and preliminary crystallographic analysis of DehI, a group I alpha-haloacid dehalogenase from Pseudomonas putida strain PP3.
• Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus.
• Smoking and alcoholism target genes associated with plasticity and glutamate transmission in the human ventral tegmental area.
• The Crystal Structure of DehI Reveals a New alpha-Haloacid Dehalogenase Fold and Active-Site Mechanism.
• The effect of chronic ethanol feeding on cytokines in a rat model of alcoholic liver disease.