Crystal Structure of an Anti-Lewis a Fab Determined by Molecular Replacement Methods

Jacqueline Vitali; William W. Young; Virginia B. Schatz; Stanley E. Sobottka; Robert H. Kretsinger

doi:10.1016/0022-2836(87)90318-4

Crystal Structure of an Anti-Lewis a Fab Determined by Molecular Replacement Methods

Jacqueline Vitali
, William W. Young
, Virginia B. Schatz
, Stanley E. Sobottka
, Robert H. Kretsinger

University of Virginia
University of Virgina

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

Abstract

The anti-Lewis a mouse immunoglobulin CF4C4 (IgGl, κ) Fab has been crystallized from 58% saturated ammonium sulfate in space group P1; unit cell dimensions a = 43.4 A b = 41.7 A , c = 62.0 A , α = 72.7 ^o, β = 96.6 ^o, γ = 100.1 ^o. X-ray diffraction data have been measured beyond 3.0 A Bragg spacing. The crystal structure has been determined by molecular replacement methods, using as search models the constant and variable domains of the mouse immunoglobulin McPC603 (IgA, κ) Fab. The crystallographic residual for the data 5.0 to 4.0 A, is 0.47. The approximate 2-fold axis relating the VL and the VH domains forms an angle of 164 ^o with the 2-fold axis relating the constant domains. The crystal packing is reasonable.

Original language	American English
Journal	Journal of Molecular Biology
Volume	198
DOIs	https://doi.org/10.1016/0022-2836(87)90318-4
State	Published - Nov 20 1987

Disciplines

Atomic, Molecular and Optical Physics
Biological and Chemical Physics

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Cite this

@article{8647d94822e542bd97420641891fe119,

title = "Crystal Structure of an Anti-Lewis a Fab Determined by Molecular Replacement Methods",

abstract = " The anti-Lewis a mouse immunoglobulin CF4C4 (IgGl, κ) Fab has been crystallized from 58\% saturated ammonium sulfate in space group P1; unit cell dimensions a = 43.4 A b = 41.7 A , c = 62.0 A , α = 72.7 \textasciicircum{}o, β = 96.6 \textasciicircum{}o, γ = 100.1 \textasciicircum{}o. X-ray diffraction data have been measured beyond 3.0 A Bragg spacing. The crystal structure has been determined by molecular replacement methods, using as search models the constant and variable domains of the mouse immunoglobulin McPC603 (IgA, κ) Fab. The crystallographic residual for the data 5.0 to 4.0 A, is 0.47. The approximate 2-fold axis relating the VL and the VH domains forms an angle of 164 \textasciicircum{}o with the 2-fold axis relating the constant domains. The crystal packing is reasonable.",

author = "Jacqueline Vitali and Young, \{William W.\} and Schatz, \{Virginia B.\} and Sobottka, \{Stanley E.\} and Kretsinger, \{Robert H.\}",

note = "Vital, J., et al. 1987. Crystal structure of an anti-Lewis a Fab determined by molecular replacement methods. Journal of Molecular Biology 198, no. 2:351-355.",

year = "1987",

month = nov,

day = "20",

doi = "10.1016/0022-2836(87)90318-4",

language = "American English",

volume = "198",

journal = "Journal of Molecular Biology",

}

TY - JOUR

T1 - Crystal Structure of an Anti-Lewis a Fab Determined by Molecular Replacement Methods

AU - Vitali, Jacqueline

AU - Young, William W.

AU - Schatz, Virginia B.

AU - Sobottka, Stanley E.

AU - Kretsinger, Robert H.

N1 - Vital, J., et al. 1987. Crystal structure of an anti-Lewis a Fab determined by molecular replacement methods. Journal of Molecular Biology 198, no. 2:351-355.

PY - 1987/11/20

Y1 - 1987/11/20

N2 - The anti-Lewis a mouse immunoglobulin CF4C4 (IgGl, κ) Fab has been crystallized from 58% saturated ammonium sulfate in space group P1; unit cell dimensions a = 43.4 A b = 41.7 A , c = 62.0 A , α = 72.7 ^o, β = 96.6 ^o, γ = 100.1 ^o. X-ray diffraction data have been measured beyond 3.0 A Bragg spacing. The crystal structure has been determined by molecular replacement methods, using as search models the constant and variable domains of the mouse immunoglobulin McPC603 (IgA, κ) Fab. The crystallographic residual for the data 5.0 to 4.0 A, is 0.47. The approximate 2-fold axis relating the VL and the VH domains forms an angle of 164 ^o with the 2-fold axis relating the constant domains. The crystal packing is reasonable.

AB - The anti-Lewis a mouse immunoglobulin CF4C4 (IgGl, κ) Fab has been crystallized from 58% saturated ammonium sulfate in space group P1; unit cell dimensions a = 43.4 A b = 41.7 A , c = 62.0 A , α = 72.7 ^o, β = 96.6 ^o, γ = 100.1 ^o. X-ray diffraction data have been measured beyond 3.0 A Bragg spacing. The crystal structure has been determined by molecular replacement methods, using as search models the constant and variable domains of the mouse immunoglobulin McPC603 (IgA, κ) Fab. The crystallographic residual for the data 5.0 to 4.0 A, is 0.47. The approximate 2-fold axis relating the VL and the VH domains forms an angle of 164 ^o with the 2-fold axis relating the constant domains. The crystal packing is reasonable.

UR - https://engagedscholarship.csuohio.edu/sciphysics_facpub/174

UR - http://journals.ohiolink.edu/ejc/article.cgi?issn=00222836issue=v198i0002article=351_csoaaafdbmrm

U2 - 10.1016/0022-2836(87)90318-4

DO - 10.1016/0022-2836(87)90318-4

M3 - Article

VL - 198

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

ER -

Crystal Structure of an Anti-Lewis a Fab Determined by Molecular Replacement Methods

Abstract

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