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pro vyhledávání: '"J.M. Guss"'
Autor:
J.M. Guss, Brian McMahon
Publikováno v:
Acta Crystallographica Section D: Biological Crystallography
An analysis is performed of the technical and financial challenges to be overcome if deposition of primary experimental data is to become routine.
The IUCr Diffraction Data Deposition Working Group is investigating the rationale and policies for
The IUCr Diffraction Data Deposition Working Group is investigating the rationale and policies for
Publikováno v:
Acta Crystallographica Section F Structural Biology Communications. 70:1032-1037
Adult haemoglobin (Hb) is made up of two α and two β subunits. Mutations that reduce expression of the α- or β-globin genes lead to the conditions α- or β-thalassaemia, respectively. Whilst both conditions are characterized by anaemia of variab
Autor:
C.D. Artuz, David A. Jacques, David J. Segal, Jacqueline M. Matthews, Merlin Crossley, Marylène Vandevenne, Ann H. Kwan, J.M. Guss, Joel P. Mackay, Cuong D. Nguyen
Publikováno v:
Journal of Biological Chemistry. 288:10616-10627
Classical zinc fingers (ZFs) are one of the most abundant and best characterized DNA-binding domains. Typically, tandem arrays of three or more ZFs bind DNA target sequences with high affinity and specificity, and the mode of DNA recognition is suffi
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 68:620-626
Small-angle scattering is becoming a mainstream technique for structural molecular biology. As such, it is important to establish guidelines for publication that will ensure that there is adequate reporting of the data and its treatment so that revie
Autor:
J.M. Guss, Jill Trewhella
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 73:C1444-C1444
Autor:
J.M. Guss, David A. Jacques, Glenn F. King, M. Streamer, David B. Langley, Jill Trewhella, Susan Rowland
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 65:574-581
The crystal structure of the DNA-damage checkpoint inhibitor of sporulation, Sda, from Bacillus subtilis, has been solved by the MAD technique using selenomethionine-substituted protein. The structure closely resembles that previously solved by NMR,
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Autor:
Anthony P. Duff, Kimberly M. Hilmer, Aina E. Cohen, J.M. Guss, Hans C. Freeman, Paul J. Ellis, David M. Dooley, David B. Langley
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 62:1073-1084
The structure of Pichia pastoris lysyl oxidase (PPLO) in a new crystal form has been refined at 1.23 A resolution. PPLO, a copper amine oxidase (CuAO) with a 2,4,5-trihydroxyphenylalanine quinone (TPQ) cofactor, differs from most other members of the
Autor:
Hans C. Freeman, H.B. Jeon, Lawrence M. Sayre, David B. Langley, J.M. Guss, Gang Sun, Anthony P. Duff, Eric M. Shepard, David M. Dooley, K.M. O'Connell
Publikováno v:
Biochemistry. 43:10965-10978
A series of compounds derived from a previously identified substrate analogue of copper amine oxidases (CuAOs) (Shepard et al. (2002) Eur. J. Biochem. 269, 3645-3658) has been screened against six different CuAOs with a view to designing potent and s
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 59:1545-1550
The structure of auracyanin B, a 'blue' copper protein produced by Chloroflexus aurantiacus, has previously been solved and refined in the hexagonal space group P6(4)22 with a single molecule in the asymmetric unit. The protein has now been crystalli