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Purification, crystallization and preliminary X-ray diffraction analysis of a variant of the ColE1 Rop protein.

ABSTRACT: Rop is the paradigm of a canonical four-alpha-helical bundle. Its loop region has attracted considerable interest because a single alanine-to-proline substitution (A31P) in the loop is sufficient to change the topology of this small protein. In order to further analyse the loop region as a possible folding-control element, the double mutant D30P/A31G (RopPG) was produced, purified and crystallized. The crystals belonged to space group P2(1), with unit-cell parameters a = 26.7, b = 38.8, c = 56.6 A, beta = 100.9 degrees and two molecules in the asymmetric unit. A complete data set was collected at 100 K to a resolution of 1.4 A using synchrotron radiation.

SUBMITTER: Ambrazi M

PROVIDER: S-EPMC2376389 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary X-ray diffraction analysis of a variant of the ColE1 Rop protein.

Ambrazi Maria M Fellas George G Kapetaniou Evangelia G EG Kotsifaki Dina D Providaki Mary M Kokkinidis Michael M

Acta crystallographica. Section F, Structural biology and crystallization communications 20080430 Pt 5

Rop is the paradigm of a canonical four-alpha-helical bundle. Its loop region has attracted considerable interest because a single alanine-to-proline substitution (A31P) in the loop is sufficient to change the topology of this small protein. In order to further analyse the loop region as a possible folding-control element, the double mutant D30P/A31G (RopPG) was produced, purified and crystallized. The crystals belonged to space group P2(1), with unit-cell parameters a = 26.7, b = 38.8, c = 56.6 ...[more]

PMID: 18453719

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