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Page 1
Isolation of monomeric human V(H)s by a phage selection.
To R, Hirama T, Arbabi-Ghahroudi M, MacKenzie R, Wang P, Xu P, Ni F, Tanha J. To R, et al. J Biol Chem. 2005 Dec 16;280(50):41395-403. doi: 10.1074/jbc.M509900200. Epub 2005 Oct 12. J Biol Chem. 2005. PMID: 16221664 Free article.
Crystallization of recombinant rat cathepsin B.
Lee X, Ahmed FR, Hirama T, Huber CP, Rose DR, To R, Hasnain S, Tam A, Mort JS. Lee X, et al. Among authors: to r. J Biol Chem. 1990 Apr 15;265(11):5950-1. J Biol Chem. 1990. PMID: 2180938 Free article.
Evidence for the extended helical nature of polysaccharide epitopes. The 2.8 A resolution structure and thermodynamics of ligand binding of an antigen binding fragment specific for alpha-(2-->8)-polysialic acid.
Evans SV, Sigurskjold BW, Jennings HJ, Brisson JR, To R, Tse WC, Altman E, Frosch M, Weisgerber C, Kratzin HD, et al. Evans SV, et al. Among authors: to r. Biochemistry. 1995 May 23;34(20):6737-44. doi: 10.1021/bi00020a019. Biochemistry. 1995. PMID: 7538787
The structure was solved by molecular replacement methods and refined to a conventional R factor of 0.164 for data to 2.8 A. The binding site is observed to display a shape and distribution of charges that is complementary to that of the predict …
The structure was solved by molecular replacement methods and refined to a conventional R factor of 0.164 for data to 2 …
Refinement of recombinant oncomodulin at 1.30 A resolution.
Ahmed FR, Rose DR, Evans SV, Pippy ME, To R. Ahmed FR, et al. Among authors: to r. J Mol Biol. 1993 Apr 20;230(4):1216-24. doi: 10.1006/jmbi.1993.1237. J Mol Biol. 1993. PMID: 8487302
A refinement of the oncomodulin crystal structure at 1.30 A resolution has been carried out with X-ray data from the recombinant protein. The crystallographic R-factor values are 0.169 for 19,995 reflections in the range 6.0 to 1.30 A, which were used for the restra …
A refinement of the oncomodulin crystal structure at 1.30 A resolution has been carried out with X-ray data from the recombinant protein. Th …
Exploring the mimicry of polysaccharide antigens by anti-idiotypic antibodies. The crystallization, molecular replacement, and refinement to 2.8 A resolution of an idiotope-anti-idiotope Fab complex and of the unliganded anti-idiotope Fab.
Evans SV, Rose DR, To R, Young NM, Bundle DR. Evans SV, et al. Among authors: to r. J Mol Biol. 1994 Sep 2;241(5):691-705. doi: 10.1006/jmbi.1994.1544. J Mol Biol. 1994. PMID: 8071993
The structure was solved using a limited Patterson-correlation search over the asymmetric-unit of rotation space, and has been refined to an R-factor of 0.174. The complex is a head-to-head dimer, with the contact between the two Fabs almost completely restri …
The structure was solved using a limited Patterson-correlation search over the asymmetric-unit of rotation space, and has been refined to …
61 results