Crystallization and preliminary cryogenic X-ray diffraction analyses of protein L-isoaspartyl O-methyltransferase from human fetal brain

C D Smith; J Barchue; C Mentel; L DeLucas; T Shirasawa; D Chattopadhyay

Crystallization and preliminary cryogenic X-ray diffraction analyses of protein L-isoaspartyl O-methyltransferase from human fetal brain

Proteins. 1997 Jul;28(3):457-60.

Authors

C D Smith¹, J Barchue, C Mentel, L DeLucas, T Shirasawa, D Chattopadhyay

Affiliation

¹ Center for Macromolecular Crystallography, University of Alabama at Birmingham, USA.

PMID: 9223191

Abstract

Recombinant human fetal brain protein L-isoaspartyl O-methyltransferase, EC 2.1.1.77, was crystallized in PEG 8000 with adenosine homocysteine by a macroseeding technique. The space group was P2(1) with a = 47.4 A, b = 53.9 A, c = 48.7 A and beta = 116.4 degrees for cryofrozen crystals at 90 K. The crystals diffracted to 2.1 A and have one molecule per asymmetric unit.

Publication types

Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Brain Chemistry*
Crystallization
Crystallography, X-Ray
Fetus
Humans
Molecular Sequence Data
Protein D-Aspartate-L-Isoaspartate Methyltransferase
Protein Methyltransferases / chemistry*

Substances

Protein Methyltransferases
Protein D-Aspartate-L-Isoaspartate Methyltransferase

Associated data

GENBANK/D13892