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PDBsum entry 2qpe

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Oxidoreductase PDB id
2qpe
Jmol
Contents
Protein chains
557 a.a.
166 a.a.
33 a.a.
Ligands
HEM
HAS
CUA
Metals
CU1

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
Abstract
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
PROCHECK
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 Headers