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2013

Journal Article

The structure of the caspase recruitment domain of BinCARD reveals that all three cysteines can be oxidized

Chen, Kai-En, Richards, Ayanthi A., Caradoc-Davies, Tom T., Vajjhala, Parimala R., Robin, Gautier, Lua, Linda H. L., Hill, Justine M., Schroder, Kate, Sweet, Matthew J., Kellie, Stuart, Kobe, Bostjan and Martin, Jennifer (2013). The structure of the caspase recruitment domain of BinCARD reveals that all three cysteines can be oxidized. Acta Crystallographica Section D: Biological Crystallography, 69 (5), 774-784. doi: 10.1107/S0907444913001558

The structure of the caspase recruitment domain of BinCARD reveals that all three cysteines can be oxidized

2012

Journal Article

The 1.2 A resolution crystal structure of TcpG, the Vibrio cholerae DsbA disulfide-forming protein required for pilus and cholera-toxin production

Walden, Patricia M., Heras, Begona, Chen, Kai-En, Halili, Maria A., Rimmer, Kieran, Sharma, Pooja, Scanlon, Martin J. and Martin, Jennifer L. (2012). The 1.2 A resolution crystal structure of TcpG, the Vibrio cholerae DsbA disulfide-forming protein required for pilus and cholera-toxin production. Acta Crystallographica Section D-Biological Crystallography, 68 (10), 1290-1302. doi: 10.1107/S0907444912026388

The 1.2 A resolution crystal structure of TcpG, the Vibrio cholerae DsbA disulfide-forming protein required for pilus and cholera-toxin production

2012

Journal Article

The mammalian DUF59 protein Fam96a forms two distinct types of domain-swapped dimer

Chen, Kai-En, Richards, Ayanthi A., Arrifin, Juliana K., Ross, Ian L., Sweet, Matthew J., Kellie, Stuart, Kobe, Bostjan and Martin, Jennifer L. (2012). The mammalian DUF59 protein Fam96a forms two distinct types of domain-swapped dimer. Acta Crystallographica Section D: Biological Crystallography, 68 (6), 637-648. doi: 10.1107/S0907444912006592

The mammalian DUF59 protein Fam96a forms two distinct types of domain-swapped dimer

2012

Journal Article

Low-resolution solution structures of Munc18: Syntaxin protein complexes indicate an open binding mode driven by the Syntaxin N-peptide

Christie, Michelle P., Whitten, Andrew E., King, Gordon J., Hu, Shu-Hong, Jarrott, Russell J., Chen, Kai-En, Duff, Anthony P., Callow, Philip, Collins, Brett M., James, David E. and Martin, Jennifer L. (2012). Low-resolution solution structures of Munc18: Syntaxin protein complexes indicate an open binding mode driven by the Syntaxin N-peptide. Proceedings of the National Academy of Sciences of the United States of America, 109 (25), 9816-9821. doi: 10.1073/pnas.1116975109

Low-resolution solution structures of Munc18: Syntaxin protein complexes indicate an open binding mode driven by the Syntaxin N-peptide

2012

Journal Article

Backbone resonance assignments of the monomeric DUF59 domain of human Fam96a

Mas, Caroline, Chen, Kai-En, Brereton, Ian M., Martin, Jennifer L. and Hill, Justine M. (2012). Backbone resonance assignments of the monomeric DUF59 domain of human Fam96a. Biomolecular NMR Assignments, 7 (2), 117-120. doi: 10.1007/s12104-012-9390-1

Backbone resonance assignments of the monomeric DUF59 domain of human Fam96a

2009

Journal Article

Interaction between plate make and protein in protein crystallisation screening

King, Gordon J., Chen, Kai-En, Robin, Gautier, Forwood, Jade K., Heras, Begoña, Thakur, Anil S., Kobe, Bostjan, Blomberg, Simon P. and Martin, Jennifer L. (2009). Interaction between plate make and protein in protein crystallisation screening. PLoS One, 4 (11) e7851, x-x. doi: 10.1371/journal.pone.0007851

Interaction between plate make and protein in protein crystallisation screening