Neutron crystallographic studies of T4 lysozyme at cryogenic temperature-Reference-Cited by-同舟云学术

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Neutron crystallographic studies of T4 lysozyme at cryogenic temperature

Published:2017-09-06 Issue:10 Volume:26 Page:2098-2104
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Li Le¹,Shukla Shantanu¹²,Meilleur Flora¹³,Standaert Robert F.⁴,Pierce Josh¹,Myles Dean A. A.¹²,Cuneo Matthew J.¹

Affiliation:

1. Oak Ridge National LaboratoryNeutron Sciences Directorate, Oak Ridge Tennessee37831

2. Genome Science and Technology, University of TennesseeKnoxville Tennessee37996

3. Department of Molecular and Structural BiochemistryNorth Carolina State UniversityRaleigh North Carolina27695

4. Energy and Environmental Sciences DirectorateOak Ridge National LaboratoryOak Ridge Tennessee37831

Funder

NSF

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.3231

Reference25 articles.

1. Structure of bacteriophage T4 lysozyme refined at 1.7 Å resolution

2. Lessons from the lysozyme of phage T4

3. Use of an ion‐binding site to bypass the 1000‐atom limit to structure determination by direct methods;Mooers BHM;Acta Cryst,2004

4. Neutron protein crystallography: current status and a brighter future

5. Neutron protein crystallography: A complementary tool for locating hydrogens in proteins

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2. Cryotrapping peroxide in the active site of human mitochondrial manganese superoxide dismutase crystals for neutron diffraction;Acta Crystallographica Section F Structural Biology Communications;2022-01-01

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4. Preliminary results of neutron and X-ray diffraction data collection on a lytic polysaccharide monooxygenase under reduced and acidic conditions;Acta Crystallographica Section F Structural Biology Communications;2021-03-31

5. Complementary Information from Neutron Crystallography Studies;Structural Biology in Drug Discovery;2020-01-02

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