Work

Thermostable multicopper oxidase from Thermus thermophilus HB27: crystallization and preliminary X-ray diffraction analysis of apo and holo forms

Year: 2011

Type: article

Abstract: A thermostable multicopper oxidase from Thermus thermophilus HB27 (Tth-MCO) was successfully crystallized using the sitting-drop and hanging-drop vapour-diffusion methods. Crystallization conditions and preliminary X-ray diffraction data to 1.5 Å resolution obtained using synchrotron radiation at 100 K are reported. The crystals belonged to space group C222(1), with unit-cell parameters a = 93.6, b = 110.3, c = 96.3 Å. A monomer in the asymmetric unit yielded a Matthews coefficient (V(M)) of 2.60 Å(3) Da(-1) and a solvent content of 53%. An inactive enzyme form, apo-Tth-MCO, was also crystallized and diffraction data were collected to 1.7 Å resolution. In addition, a second inactive form of the enzyme, Hg-Tth-MCO, was obtained by soaking apo-Tth-MCO crystals with mercury(II) chloride and data were collected to a resolution of 1.7 Å.

Source: Acta Crystallographica Section F Structural Biology and Crystallization Communications

DOI: 10.1107/s174430911103805x

Authors: Hugo Serrano-Posada, Brenda Valderrama, Vivian Stojanoff, Enrique Rudiño-Piñera

Institutions: Universidad Nacional Autónoma de México, Brookhaven National Laboratory

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: bronze

Funder: National Institute of General Medical Sciences

Award: G357077679