L. Cunane

X-ray structure of the cupredoxin amicyanin, from Paracoccus denitrificans, refined at 1.31 A resolution.

F. S. Mathews, Z. Chen, Z W Chen, 1996, Acta crystallographica. Section D, Biological crystallography.

Molecular basis for interprotein complex-dependent effects on the redox properties of amicyanin.

F. S. Mathews, V. Davidson, Z. Chen, 1998, Biochemistry.

The Cytochrome Subunit Is Necessary for Covalent FAD Attachment to the Flavoprotein Subunit of p-Cresol Methylhydroxylase (*)

F. S. Mathews, Z. Chen, W. McIntire, 1995, The Journal of Biological Chemistry.

Experimental charge density and electrostatic potential in adenine hydrochloride hemihydrate at 123 K

L. Cunane, M. Taylor, 1993 .

Crystal structure analysis of recombinant rat kidney long chain hydroxy acid oxidase.

F. S. Mathews, F. Lederer, D. Amar, 2005, Biochemistry.

Crystallographic study of the recombinant flavin-binding domain of Baker's yeast flavocytochrome b(2): comparison with the intact wild-type enzyme.

S. Chapman, L. Cunane, G. Reid, 2002, Biochemistry.

Flavin electron transfer proteins.

R. Durley, L. Cunane, F. Mathews, 2000, Sub-cellular biochemistry.

Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: gated substrate entry and proton relays support the proposed catalytic mechanism.

Z. Chen, W. McIntire, L. Cunane, 2000, Journal of molecular biology.