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

Abstract

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.

Authors:
 [1]; ;  [2]
  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)
Publication Date:
OSTI Identifier:
22472327
Resource Type:
Journal Article
Journal Name:
Crystallography Reports
Additional Journal Information:
Journal Volume: 60; Journal Issue: 3; Other Information: Copyright (c) 2015 Pleiades Publishing, Inc.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1063-7745
Country of Publication:
United States
Language:
English
Subject:
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

Citation Formats

Akparov, V. Kh., E-mail: valery@akparov.ru, Timofeev, V. I., E-mail: inna@ns.crys.ras.ru, and Kuranova, I. P., E-mail: tostars@mail.ru. Crystallization and preliminary X-ray diffraction study of porcine carboxypeptidase B. United States: N. p., 2015. Web. doi:10.1134/S1063774515030025.
Akparov, V. Kh., E-mail: valery@akparov.ru, Timofeev, V. I., E-mail: inna@ns.crys.ras.ru, & Kuranova, I. P., E-mail: tostars@mail.ru. Crystallization and preliminary X-ray diffraction study of porcine carboxypeptidase B. United States. doi:10.1134/S1063774515030025.
Akparov, V. Kh., E-mail: valery@akparov.ru, Timofeev, V. I., E-mail: inna@ns.crys.ras.ru, and Kuranova, I. P., E-mail: tostars@mail.ru. Fri . "Crystallization and preliminary X-ray diffraction study of porcine carboxypeptidase B". United States. doi:10.1134/S1063774515030025.
@article{osti_22472327,
title = {Crystallization and preliminary X-ray diffraction study of porcine carboxypeptidase B},
author = {Akparov, V. Kh., E-mail: valery@akparov.ru and Timofeev, V. I., E-mail: inna@ns.crys.ras.ru and Kuranova, I. P., E-mail: tostars@mail.ru},
abstractNote = {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.},
doi = {10.1134/S1063774515030025},
journal = {Crystallography Reports},
issn = {1063-7745},
number = 3,
volume = 60,
place = {United States},
year = {2015},
month = {5}
}