Published May 2015
| Version v1
Journal article
Crystallization and preliminary X-ray diffraction study of porcine carboxypeptidase B
- 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)
Description
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. P41212 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
Additional details
Identifiers
Publishing Information
- Journal Title
- Crystallography Reports
- Journal Volume
- 60
- Journal Issue
- 3
- Journal Page Range
- p. 367-369
- ISSN
- 1063-7745
- CODEN
- CYSTE3
INIS
- Country of Publication
- United States
- Country of Input or Organization
- International Atomic Energy Agency (IAEA)
- INIS RN
- 47042141
- Subject category
- S75: CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY;
- Descriptors DEI
- CARBOXYPEPTIDASES; CRYSTAL GROWTH; CRYSTALLIZATION; CRYSTALS; DIFFUSION; LAYERS; PANCREAS; RESOLUTION; SPRING-8 STORAGE RING; TETRAGONAL LATTICES; WEIGHTLESSNESS; X-RAY DIFFRACTION
- Descriptors DEC
- BODY; COHERENT SCATTERING; CRYSTAL LATTICES; CRYSTAL STRUCTURE; DIFFRACTION; DIGESTIVE SYSTEM; ENDOCRINE GLANDS; ENZYMES; GLANDS; HYDROLASES; ORGANIC COMPOUNDS; ORGANS; PEPTIDE HYDROLASES; PHASE TRANSFORMATIONS; PROTEINS; RADIATION SOURCES; SCATTERING; STORAGE RINGS; SYNCHROTRON RADIATION SOURCES; THREE-DIMENSIONAL LATTICES
Optional Information
- Copyright
- Copyright (c) 2015 Pleiades Publishing, Inc.