Crystallization and preliminary crystallographic analysisof Streptomyces griseus aminopeptidase

Orna Almog; Harry M. Greenblatt; Ania Spangin; Daniella Ben-Meir; Shmaryahu Blumberg; Gil Shoham

doi:10.1006/jmbi.1993.1146

Crystallization and preliminary crystallographic analysisof Streptomyces griseus aminopeptidase

Orna Almog, Harry M. Greenblatt, Ania Spangin, Daniella Ben-Meir, Shmaryahu Blumberg, Gil Shoham

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

19 Scopus citations

Abstract

Streptomyces griseus excretes a small molecular mass (30 kDa) aminopeptidase that could be used for various biotechnological applications. This enzyme was isolated from an extracellular protease mixture of Streptomyces griseus (Pronase E, Sigma) and single crystals were obtainedby the vapor diffusion method using polyethylene glycol 4000 as the precipitant. The crystals belong to the tetragonal space group P4₁2₁2 (P4₃2₁2), with cell dimensions of a = b = 61·82(3) Å and c = 145·88(4) Å. Thesecrystals are mechanically strong, they are stable in the X-ray beam and they diffract to better than 1·8 Å resolution. The cell dimensions and the cell symmetry are consistent with one molecule in the asymmetric unit and the crystals are suitable for a detailed high-resolution crystallographic analysis. A complete nativedata set to 1·9 Å resolution has been collected on a Rigaku R-AXIS-IIC Imaging Plate Detector system and a heavy-atom derivative search is in progress.

Original language	English
Pages (from-to)	342-344
Number of pages	3
Journal	Journal of Molecular Biology
Volume	230
Issue number	1
DOIs	https://doi.org/10.1006/jmbi.1993.1146
State	Published - 5 Mar 1993
Externally published	Yes

Keywords

Aminopeptidase
Crystallization
Streptomyces griseus
X-ray analysis

ASJC Scopus subject areas

Biophysics
Structural Biology
Molecular Biology

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10.1006/jmbi.1993.1146

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title = "Crystallization and preliminary crystallographic analysisof Streptomyces griseus aminopeptidase",

abstract = "Streptomyces griseus excretes a small molecular mass (30 kDa) aminopeptidase that could be used for various biotechnological applications. This enzyme was isolated from an extracellular protease mixture of Streptomyces griseus (Pronase E, Sigma) and single crystals were obtainedby the vapor diffusion method using polyethylene glycol 4000 as the precipitant. The crystals belong to the tetragonal space group P41212 (P43212), with cell dimensions of a = b = 61·82(3) {\AA} and c = 145·88(4) {\AA}. Thesecrystals are mechanically strong, they are stable in the X-ray beam and they diffract to better than 1·8 {\AA} resolution. The cell dimensions and the cell symmetry are consistent with one molecule in the asymmetric unit and the crystals are suitable for a detailed high-resolution crystallographic analysis. A complete nativedata set to 1·9 {\AA} resolution has been collected on a Rigaku R-AXIS-IIC Imaging Plate Detector system and a heavy-atom derivative search is in progress.",

keywords = "Aminopeptidase, Crystallization, Streptomyces griseus, X-ray analysis",

author = "Orna Almog and Greenblatt, {Harry M.} and Ania Spangin and Daniella Ben-Meir and Shmaryahu Blumberg and Gil Shoham",

year = "1993",

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doi = "10.1006/jmbi.1993.1146",

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T1 - Crystallization and preliminary crystallographic analysisof Streptomyces griseus aminopeptidase

AU - Almog, Orna

AU - Greenblatt, Harry M.

AU - Spangin, Ania

AU - Ben-Meir, Daniella

AU - Blumberg, Shmaryahu

AU - Shoham, Gil

PY - 1993/3/5

Y1 - 1993/3/5

N2 - Streptomyces griseus excretes a small molecular mass (30 kDa) aminopeptidase that could be used for various biotechnological applications. This enzyme was isolated from an extracellular protease mixture of Streptomyces griseus (Pronase E, Sigma) and single crystals were obtainedby the vapor diffusion method using polyethylene glycol 4000 as the precipitant. The crystals belong to the tetragonal space group P41212 (P43212), with cell dimensions of a = b = 61·82(3) Å and c = 145·88(4) Å. Thesecrystals are mechanically strong, they are stable in the X-ray beam and they diffract to better than 1·8 Å resolution. The cell dimensions and the cell symmetry are consistent with one molecule in the asymmetric unit and the crystals are suitable for a detailed high-resolution crystallographic analysis. A complete nativedata set to 1·9 Å resolution has been collected on a Rigaku R-AXIS-IIC Imaging Plate Detector system and a heavy-atom derivative search is in progress.

AB - Streptomyces griseus excretes a small molecular mass (30 kDa) aminopeptidase that could be used for various biotechnological applications. This enzyme was isolated from an extracellular protease mixture of Streptomyces griseus (Pronase E, Sigma) and single crystals were obtainedby the vapor diffusion method using polyethylene glycol 4000 as the precipitant. The crystals belong to the tetragonal space group P41212 (P43212), with cell dimensions of a = b = 61·82(3) Å and c = 145·88(4) Å. Thesecrystals are mechanically strong, they are stable in the X-ray beam and they diffract to better than 1·8 Å resolution. The cell dimensions and the cell symmetry are consistent with one molecule in the asymmetric unit and the crystals are suitable for a detailed high-resolution crystallographic analysis. A complete nativedata set to 1·9 Å resolution has been collected on a Rigaku R-AXIS-IIC Imaging Plate Detector system and a heavy-atom derivative search is in progress.

KW - Aminopeptidase

KW - Crystallization

KW - Streptomyces griseus

KW - X-ray analysis

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DO - 10.1006/jmbi.1993.1146

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SN - 0022-2836

VL - 230

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JO - Journal of Molecular Biology

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IS - 1

ER -

Crystallization and preliminary crystallographic analysisof Streptomyces griseus aminopeptidase

Abstract

Keywords

ASJC Scopus subject areas

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