S.E. Sedelnikova

University of Sheffield

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Patrick J. Baker

University of Sheffield

D.W. Rice

Stanford University

John B. Rafferty

University of Sheffield

S.N. Ruzheinikov

University of Sheffield

David W. Rice

National University of Malaysia

G.M. Blackburn

University of Sheffield

Jon R. Sayers

University of Sheffield

Timothy J. Stillman

University of Sheffield

Iain A. Murray

New England Biolabs (United States)

T. A. Muranova

Lomonosov Moscow State University

Cooperative Institutions

University of Sheffield

Newcastle University

Jubilant Life Sciences (India)

Durham University

Prolysis (United Kingdom)

University of Manchester

Centre National de la Recherche Scientifique

University of Oxford

AstraZeneca (United Kingdom)

MRC Laboratory of Molecular Biology

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Crystal structure of IGPD from Pyrococcus furiosus in complex with (R)-C348

C. Bisson K.L. Britton S.E. Sedelnikova H. Fiona Rodgers T.C. Eadsforth

Pyrococcus furiosus

10.2210/pdb5dnl/pdb

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Molecular basis for inhibition and resistance of glutamate racemase to a family of D-glu analogues

Acta Crystallographica Section A Foundations of Crystallography (2008)

Christine Davies S.N. Ruzheinikov S.E. Sedelnikova Patrick J. Baker D.W. Rice

Human carbonic anhydrases are potential drug targets for a number of diseases.One of the novel applications is to use some of their isozymes as anti-cancer drug targets.Structure-thermodynamic property relations of novel hCA thiadiazole class inhibitors with a triple-ring system bound to hCAII will be discussed.Structures of several inhibitors are solved to atomic resolution using X-ray diffraction of hCAII-inhibitor complex crystals.The structural data are correlated with the isothermal titration calorimetry measurements.The calorimetric data together with the structures provide insight into the structural base of the tight and selective hCA inhibitor binding.

10.1107/s0108767308088855

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The structure of wt A. thaliana IGPD2 in complex with Mn2+ and phosphate

C. Bisson K.L. Britton S.E. Sedelnikova H. Fiona Rodgers T.C. Eadsforth

10.2210/pdb4qnk/pdb

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Crystallization and preliminary X-ray analysis of the glycerol-3-phosphate 1-acyltransferase from squash (Cucurbita moschata)

Acta Crystallographica Section D Biological Crystallography (2001)

Andy P. Turnbull John B. Rafferty S.E. Sedelnikova Antoni R. Slabas Ted Schierer

Glycerol-3-phosphate 1-acyltransferase (E.C. 2.3.1.15; G3PAT) catalyses the incorporation of an acyl group from either acyl-acyl carrier proteins (acylACPs) or acylCoAs into the sn-1 position of glycerol 3-phosphate to yield 1-acylglycerol 3-phosphate. Crystals of squash G3PAT have been obtained by the hanging-drop method of vapour diffusion using PEG 4000 as the precipitant. These crystals are most likely to belong to space group P212121, with approximate unit-cell parameters a = 61.1, b = 65.1, c = 103.3 Å, α = β = γ = 90° and a monomer in the asymmetric unit. X-ray diffraction data to 1.9 Å resolution have been collected in-house using a MAR 345 imaging-plate system.

Squash

Acyltransferases

Cucurbita moschata

10.1107/s0907444901000257

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Citations (8)

HIGH RESOLUTION CRYSTAL STRUCTURE OF THE COMPLEX OF THE FAB FRAGMENT OF ESTEROLYTIC ANTIBODY MS6-12 AND A TRANSITION-STATE ANALOG

S.N. Ruzheinikov T. A. Muranova S.E. Sedelnikova Linda Partridge G.M. Blackburn

Fragment (logic)

Transition state analog

10.2210/pdb1mjj/pdb

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