Thermostable multicopper oxidase from Thermusthermophilus HB27: crystallization and preliminaryX-ray diffraction analysis of apo and holo forms
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 {angstrom} resolution obtained using synchrotron radiation at 100 K are reported. The crystals belonged to space group C222{sub 1}, with unit-cell parameters a = 93.6, b = 110.3, c = 96.3 {angstrom}. A monomer in the asymmetric unit yielded a Matthews coefficient (V{sub M}) of 2.60 {angstrom}{sup 3} Da{sup -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 {angstrom} 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 {angstrom}.
- Research Organization:
- Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
- Sponsoring Organization:
- USDOE SC OFFICE OF SCIENCE (SC)
- DOE Contract Number:
- DE-AC02-98CH10886
- OSTI ID:
- 1041613
- Report Number(s):
- BNL-96849-2012-JA; R&D Project: LS001; TRN: US201212%%31
- Journal Information:
- Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 67, Issue 12; ISSN 1744-3091
- Country of Publication:
- United States
- Language:
- English
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