Crystallization and Preliminary X-ray Diffraction Analysis of Hemextin A: A Unique Anticoagulant Protein from Hemachatus haemachatus Venom

doi:10.1107/S1744309107034239

Title: Crystallization and Preliminary X-ray Diffraction Analysis of Hemextin A: A Unique Anticoagulant Protein from Hemachatus haemachatus Venom

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Abstract

Hemextin A was isolated and purified from African Ringhals cobra (Hemachatus haemachatus). It is a three-finger toxin that specifically inhibits blood coagulation factor VIIa and clot formation and that also interacts with hemextin B to form a unique anticoagulant complex. Hemextin A was crystallized by the hanging-drop vapor-diffusion method by equilibration against 0.2 M ammonium acetate, 0.1 M sodium acetate trihydrate pH 4.6 and 30% PEG 4000 as the precipitating agent. The crystals belong to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 49.27, b = 49.51, c = 57.87 {angstrom} and two molecules in the asymmetric unit. They diffracted to 1.5 {angstrom} resolution at beamline X25 at BNL.

Authors:: Banerjee,Y.; Kumar, S.; Jobichen, C.; Kini, R.

Publication Date:: Mon Jan 01 00:00:00 EST 2007

Research Org.:: Brookhaven National Laboratory (BNL) National Synchrotron Light Source

Sponsoring Org.:: Doe - Office Of Science

OSTI Identifier:: 930007

Report Number(s):: BNL-80620-2008-JA
TRN: US200822%%1159

DOE Contract Number:: DE-AC02-98CH10886

Resource Type:: Journal Article

Resource Relation:: Journal Name: Acta Crystallographica Section F: Structural Biology and Crystallization Communications; Journal Volume: 63

Country of Publication:: United States

Language:: English

Subject:: 59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; ACETATES; ANTICOAGULANTS; BLOOD COAGULATION FACTORS; BNL; CRYSTALLIZATION; CRYSTALS; MOLECULES; PROTEINS; RESOLUTION; SODIUM; SPACE GROUPS; TOXINS; VENOMS; X-RAY DIFFRACTION; national synchrotron light source

Citation Formats


                    Banerjee,Y., Kumar, S., Jobichen, C., and Kini, R.. Crystallization and Preliminary X-ray Diffraction Analysis of Hemextin A: A Unique Anticoagulant Protein from Hemachatus haemachatus Venom.  United States: N. p., 2007. 
        Web.  doi:10.1107/S1744309107034239.

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                    Banerjee,Y., Kumar, S., Jobichen, C., & Kini, R.. Crystallization and Preliminary X-ray Diffraction Analysis of Hemextin A: A Unique Anticoagulant Protein from Hemachatus haemachatus Venom.  United States.  doi:10.1107/S1744309107034239.

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                    Banerjee,Y., Kumar, S., Jobichen, C., and Kini, R.. Mon .  
        "Crystallization and Preliminary X-ray Diffraction Analysis of Hemextin A: A Unique Anticoagulant Protein from Hemachatus haemachatus Venom".  United States.  
        doi:10.1107/S1744309107034239.

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@article{osti_930007,

  title        = {Crystallization and Preliminary X-ray Diffraction Analysis of Hemextin A: A Unique Anticoagulant Protein from Hemachatus haemachatus Venom},

  author       = {Banerjee,Y. and Kumar, S. and Jobichen, C. and Kini, R.},

  abstractNote = {Hemextin A was isolated and purified from African Ringhals cobra (Hemachatus haemachatus). It is a three-finger toxin that specifically inhibits blood coagulation factor VIIa and clot formation and that also interacts with hemextin B to form a unique anticoagulant complex. Hemextin A was crystallized by the hanging-drop vapor-diffusion method by equilibration against 0.2 M ammonium acetate, 0.1 M sodium acetate trihydrate pH 4.6 and 30% PEG 4000 as the precipitating agent. The crystals belong to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 49.27, b = 49.51, c = 57.87 {angstrom} and two molecules in the asymmetric unit. They diffracted to 1.5 {angstrom} resolution at beamline X25 at BNL.},

  doi          = {10.1107/S1744309107034239},

  journal      = {Acta Crystallographica Section F: Structural Biology and Crystallization Communications},

  number       = ,

  volume       = 63,

  place        = {United States},

  year         = {Mon Jan 01 00:00:00 EST 2007},

  month        = {Mon Jan 01 00:00:00 EST 2007}

}

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DOI: 10.1107/S1744309107034239

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