PDBsum entry 2qpe

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Oxidoreductase PDB id
Protein chains
557 a.a.
166 a.a.
33 a.a.

References listed in PDB file
Key reference
Title An unexpected outcome of surface engineering an integral membrane protein: improved crystallization of cytochrome ba(3) from thermus thermophilus.
Authors B.Liu, V.M.Luna, Y.Chen, C.D.Stout, J.A.Fee.
Ref. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2007, 63, 1029-1034.
PubMed id 18084085
Past work has shown that it is feasible to mutate surface residues of soluble proteins and to a lesser extent membrane proteins in order to improve their crystallization behavior. Described here is a successful application of this approach to the integral membrane protein Thermus thermophilus cytochrome ba(3) oxidase. Two mutant forms of this enzyme (I-K258R and I-K258R/II-E4Q) were created in which symmetrical crystal contacts within crystals of wild-type enzyme were modified. These mutant proteins had greatly shortened crystallization times, decreasing from approximately 30 d for the wild type to 1-3 d for the mutants, and crystallization was highly reproducible. Native-like proteins crystallize in space group P4(3)2(1)2, whereas the mutant proteins crystallize in space group P4(1)2(1)2 with a different packing arrangement. Crystals of the P4(3)2(1)2 form occasionally diffracted to 2.4-2.3 A resolution following controlled dehydration, while those of the P4(1)2(1)2 form routinely diffracted to between 3.0 and 2.6 A for crystals that had been cryoprotected but not dehydrated.
Secondary reference #1
Title A homologous expression system for obtaining engineered cytochrome ba3 from thermus thermophilus hb8.
Authors Y.Chen, L.Hunsicker-Wang, R.L.Pacoma, E.Luna, J.A.Fee.
Ref. Protein Expr Purif, 2005, 40, 299-318. [DOI no: 10.1016/j.pep.2004.11.014]
PubMed id 15766872
Full text Abstract
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