Preparation, crystallization, and preliminary X-ray diffraction study of mutant carboxypeptidase T containing the primary specificity pocket of carboxypeptidase B
- Scientific Center of Russian Federation Research Institute for Genetics and Selection of Industrial Microorganisms (Russian Federation)
- Russian Academy of Sciences, Shubnikov Institute of Crystallography (Russian Federation)
Recombinant G215S, A251G, T257A, D260G, T262D mutant carboxypeptidase T from Thermoactinomyces vulgaris containing mutations in the primary specificity pocket was prepared and crystallized. Single crystals with a size of up to 0.3 mm were grown and investigated by X-ray diffraction. Recombinant mutant carboxypeptidase T containing the primary specificity subsite compositionally identical to that of pancreatic carboxypeptidase B crystallizes in the same space group as the natural enzyme. The crystals belong to sp. gr. P6{sub 3}22; the unit-cell parameters are a = b = 157.867 A, c = 104.304 A, {alpha} = {beta} = 90 deg., {gamma} = 120 deg. X-ray diffraction data suitable for determining the three-dimensional structure at atomic resolution were collected from one crystal.
- OSTI ID:
- 22054092
- Journal Information:
- Crystallography Reports, Vol. 55, Issue 5; Other Information: Copyright (c) 2010 Pleiades Publishing, Ltd.; Country of input: International Atomic Energy Agency (IAEA); ISSN 1063-7745
- Country of Publication:
- United States
- Language:
- English
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