The structure of the pea lectin-D-mannopyranose complex at a 2.1 Å resolution

S. N. Ruzheinikov; I. Yu Mikhailova; I. N. Tsygannik; W. Pangborn; W. Duax; V. Z. Pletnev

The structure of the pea lectin-D-mannopyranose complex at a 2.1 Å resolution

S. N. Ruzheinikov
, I. Yu Mikhailova
, I. N. Tsygannik
, W. Pangborn
, W. Duax
, V. Z. Pletnev

Department of Structural Biology

Russian Academy of Sciences
Hauptman Woodward Medical Institute

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

The structure of a new crystal complex (P2₁2₁2₁ spatial group, cell dimensions: a 73.926, b 104.083, and c 64.837 Å) of pea lectin (Pisum sativum, dimer, molecular mass ca. 52 kDa) with D-mannopyranose was established by the molecular replacement approach at a resolution of 2.1 Å. After crystallographic refinement, the value of the R-factor was 16.1%. The mannose molecule was shown to be fixed by six hydrogen bonds with Asp81, Gly99, Asn125, Ala217, and Glu218.

Original language	English
Pages (from-to)	277-279
Number of pages	3
Journal	Russian Journal of Bioorganic Chemistry
Volume	24
Issue number	4
State	Published - 1998

Keywords

Crystal complex
Pea lectin
X-ray analysis

Cite this

@article{1515c69ee0454a31befe4bff817768f9,

title = "The structure of the pea lectin-D-mannopyranose complex at a 2.1 {\AA} resolution",

abstract = "The structure of a new crystal complex (P212121 spatial group, cell dimensions: a 73.926, b 104.083, and c 64.837 {\AA}) of pea lectin (Pisum sativum, dimer, molecular mass ca. 52 kDa) with D-mannopyranose was established by the molecular replacement approach at a resolution of 2.1 {\AA}. After crystallographic refinement, the value of the R-factor was 16.1\%. The mannose molecule was shown to be fixed by six hydrogen bonds with Asp81, Gly99, Asn125, Ala217, and Glu218.",

keywords = "Crystal complex, Pea lectin, X-ray analysis",

author = "Ruzheinikov, \{S. N.\} and Mikhailova, \{I. Yu\} and Tsygannik, \{I. N.\} and W. Pangborn and W. Duax and Pletnev, \{V. Z.\}",

year = "1998",

language = "English",

volume = "24",

pages = "277--279",

journal = "Russian Journal of Bioorganic Chemistry",

issn = "1068-1620",

publisher = "Pleiades Publishing",

number = "4",

}

TY - JOUR

T1 - The structure of the pea lectin-D-mannopyranose complex at a 2.1 Å resolution

AU - Ruzheinikov, S. N.

AU - Mikhailova, I. Yu

AU - Tsygannik, I. N.

AU - Pangborn, W.

AU - Duax, W.

AU - Pletnev, V. Z.

PY - 1998

Y1 - 1998

N2 - The structure of a new crystal complex (P212121 spatial group, cell dimensions: a 73.926, b 104.083, and c 64.837 Å) of pea lectin (Pisum sativum, dimer, molecular mass ca. 52 kDa) with D-mannopyranose was established by the molecular replacement approach at a resolution of 2.1 Å. After crystallographic refinement, the value of the R-factor was 16.1%. The mannose molecule was shown to be fixed by six hydrogen bonds with Asp81, Gly99, Asn125, Ala217, and Glu218.

AB - The structure of a new crystal complex (P212121 spatial group, cell dimensions: a 73.926, b 104.083, and c 64.837 Å) of pea lectin (Pisum sativum, dimer, molecular mass ca. 52 kDa) with D-mannopyranose was established by the molecular replacement approach at a resolution of 2.1 Å. After crystallographic refinement, the value of the R-factor was 16.1%. The mannose molecule was shown to be fixed by six hydrogen bonds with Asp81, Gly99, Asn125, Ala217, and Glu218.

KW - Crystal complex

KW - Pea lectin

KW - X-ray analysis

UR - https://www.scopus.com/pages/publications/0007713003

M3 - Article

AN - SCOPUS:0007713003

SN - 1068-1620

VL - 24

SP - 277

EP - 279

JO - Russian Journal of Bioorganic Chemistry

JF - Russian Journal of Bioorganic Chemistry

IS - 4

ER -

The structure of the pea lectin-D-mannopyranose complex at a 2.1 Å resolution

Abstract

Keywords

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