A preliminary crystallographic investigation of avidin.

The Biochemical journal ·Vol. 118 ·No. 1 ·1970-06-00 ·Pages 71-2

Green NM, Joynson MA

Abstract

Avidin was crystallized in various forms from 3m-ammonium sulphate or sodium phosphate at pH5.2. X-ray-crystallographic analysis of crystals from phosphate showed them to be orthorhombic, space group C222, containing two molecules per unit cell and with a single subunit as the asymmetric unit. The formation of the complex with biotin did not affect the morphology of the crystals.

MeSH Terms

Biotin Crystallization Crystallography Ovalbumin Protein Binding X-Ray Diffraction

Chemicals

Biotin Ovalbumin

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Green N M

Joynson M A

References (3)

3 references, click to expand

Solvent content of protein crystals.
J Mol Biol. 1968 Apr 28;33(2):491-7 PMID: 5700707
Purification and crystallization of avidin.
Biochem J. 1970 Jun;118(1):67-70 PMID: 5528638
AVIDIN. 4. STABILITY AT EXTREMES OF PH AND DISSOCIATION INTO SUB-UNITS BY GUANIDINE HYDROCHLORIDE.
Biochem J. 1963 Dec;89:609-20 PMID: 14101982

Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj1180071

Published

1970-06-00

Pages

71-2

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1179081

Subset

External Links

PubMed source DOI: 10.1042/bj1180071 PMC Full Text View journal details

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A preliminary crystallographic investigation of avidin.

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