Crystallization And Preliminary X-Ray Studies Of A Thermostable Dna Photolyase From Thermus Thermophilus Hb8

Authors: Komori H.; Tsujiuchi H.; Masuii R.; Kuramitsu s.; Yokoyama S.; Shibata T.; Inoue Y.; Miki K.

Source: Protein and Peptide Letters, Volume 8, Number 6, December 2001 , pp. 495-498(4)

Publisher: Bentham Science Publishers

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Abstract:

A thermostable DNA photolyase from an extremely thermophilic bacterium, Thermus thermophilus HB8 has been crystallized by the hanging drop vapor diffusion method using NH4H2PO4 as a precipitant. The hexagonal crystals were grown to a size of 0.4 mm in length. X-ray diffraction experiments show the crystals to belong to the hexagonal space group P6 5 22 or P6 1 22 with the unit cell dimensions of a=b=113.6 A, c=142.0 A. They diffract X-rays to 2.4 A resolution with synchrotron radiation.

Keywords: THERMOSTABLE DNA PHOTOLYASE; THERMUS THERMOPHILUS HB8; CPD photolyase; Escherichia coli; Anacystis nidulans

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866013409157

Publication date: 2001-12-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.