Crystallization and preliminary X-ray diffraction study of porcine carboxypeptidase B

Journal Article · Fri May 15 00:00:00 EDT 2015 · Crystallography Reports

DOI:https://doi.org/10.1134/S1063774515030025· OSTI ID:22472327

Akparov, V. Kh., E-mail: [e-mail] ^[1]; Timofeev, V. I., E-mail: [e-mail]; Kuranova, I. P., E-mail: [e-mail] ^[2]

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1. Scientific Center of Russian Federation Research Institute for Genetics and Selection of Industrial Microorganisms (Russian Federation)
2. Russian Academy of Sciences, Shubnikov Institute of Crystallography (Russian Federation)

Crystals of porcine pancreatic carboxypeptidase B have been grown in microgravity by the capillary counter-diffusion method through a gel layer. The X-ray diffraction study showed that the crystals belong to sp. gr. P4{sub 1}2{sub 1}2 and have the following unit-cell parameters: a = b = 79.58 Å, c = 100.51 Å; α = β = γ = 90.00°. The X-ray diffraction data set suitable for the determination of the three-dimensional structure at atomic resolution was collected from one of the grown crystals at the SPring 8 synchrotron facility to 0.98 Å resolution.

• OSTI ID: 22472327
• Journal Information: Crystallography Reports, Vol. 60, Issue 3; Other Information: Copyright (c) 2015 Pleiades Publishing, Inc.; Country of input: International Atomic Energy Agency (IAEA); ISSN 1063-7745
• Country of Publication: United States
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CARBOXYPEPTIDASES
CRYSTAL GROWTH
CRYSTALLIZATION
CRYSTALS
DIFFUSION
LAYERS
PANCREAS
RESOLUTION
SPRING-8 STORAGE RING
TETRAGONAL LATTICES
WEIGHTLESSNESS
X-RAY DIFFRACTION