Alexander McPherson

Scripps Research Institute

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Steven B. Larson

Memorial Sloan Kettering Cancer Center

John Day

University of California, Irvine

Aaron Greenwood

University of Groningen

Yurii G. Kuznetsov

First Pavlov State Medical University of St. Petersburg

Yu. G. Kuznetsov

University of California, Irvine

A. J. Malkin

Lawrence Livermore National Laboratory

Alexander J. Malkin

Lawrence Livermore National Laboratory

Alexander Rich

Edaptive Computing (United States)

Nenad Ban

ETH Zurich

Michael G. Rossmann

Purdue University West Lafayette

Cooperative Institutions

University of California, Riverside

University of California, Irvine

Centre National de la Recherche Scientifique

University of Alabama at Birmingham

Purdue University West Lafayette

Massachusetts Institute of Technology

Agricultural Research Organization

GTx (United States)

Cornell University

National Institutes of Health

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Mechanisms of Protein Crystal Growth: An Atomic Force Microscopy Study of Canavalin Crystallization

Physical Review Letters (1995)

T. A. Land A. J. Malkin Yu. G. Kuznetsov Alexander McPherson James J. De Yoreo

In situ atomic force microscopy has been used to investigate step dynamics and surface evolution during the growth of single crystals of canavalin, a protein with a well known structure. Growth occurs by step flow on complex dislocation hillocks, and involves the formation and incorporation of small, mobile molecular clusters. Defects in the form of hollow channels are observed and persist over growth times of several days. The results are used to establish a physical picture of the growth mechanism, and estimate the values of the free energy of the step edge, $\ensuremath{\alpha}$, and the kinetic coefficient, $\ensuremath{\beta}$.

Hillock

Protein crystallization

10.1103/physrevlett.75.2774

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Citations (117)

The structure of a DNA unwinding protein and its complexes with oligodeoxynucleotides by x-ray diffraction

Biophysical Journal (1980)

Alexander McPherson Frances Jurnak A. Wang Francis J. Kolpak Alexander Rich

Polynucleotide

Nucleobase

A-DNA

10.1016/s0006-3495(80)84931-9

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Citations (37)

First Crystallographic Structure of a Xylanase from Glycoside Hydrolase Family 5: Implications for Catalysis^,

Biochemistry (2003)

Steven B. Larson John Day A. P. Barba de la Rosa Noel T. Keen Alexander McPherson

The room-temperature structure of xylanase (EC 3.2.1.8) from the bacterial plant pathogen Erwinia chrysanthemi expressed in Escherichia coli, a 45 kDa, 413-amino acid protein belonging to glycoside hydrolase family 5, has been determined by multiple isomorphous replacement and refined to a resolution of 1.42 Å. This represents the first structure of a xylanase not belonging to either glycoside hydrolase family 10 or family 11. The enzyme is composed of two domains similar to most family 10 xylanases and the α-amylases. The catalytic domain (residues 46−315) has a (β/α)8-barrel motif with a binding cleft along the C-terminal side of the β-barrel. The catalytic residues, Glu165 and Glu253, determined by correspondence to other family 5 and family 10 glycoside hydrolases, lie inside this cleft on the C-terminal ends of β-strands 4 and 7, respectively, with an Oε2···Oε1 distance of 4.22 Å. The smaller domain (residues 31−43 and 323−413) has a β9-barrel motif with five of the strands interfacing with α-helices 7 and 8 of the catalytic domain. The first 13 N-terminal residues form one β-strand of this domain. Residues 44, 45, and 316−322 form the linkers between this domain and the catalytic domain.

Hydrolase

10.1021/bi034144c

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Citations (72)

The binding of pentaammineruthenium (III) to RNase B and RNase A+d(pA)4 in the crystalline state

Journal of Protein Chemistry (1987)

Roger Williams Herbert L. Axelrod Marie Greene Alexander McPherson

Imidazole

RNase H

Ribonuclease T1

10.1007/bf00248053

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Citations (2)

Structural Comparison of the Plant Satellite Viruses

Virology (1995)

Nenad Ban Steven B. Larson Alexander McPherson

10.1006/viro.1995.0068

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Citations (47)

Surface Processes in the Crystallization of Turnip Yellow Mosaic Virus Visualized by Atomic Force Microscopy

Journal of Structural Biology (1999)

Alexander J. Malkin Yurii G. Kuznetsov Robert W. Lucas Alexander McPherson

Cowpea mosaic virus

Crystal (programming language)

10.1006/jsbi.1999.4128

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Citations (55)

Polymeric Precipitants for the Crystallization of Macromolecules

Biochemical and Biophysical Research Communications (1995)

Sandeep Patel Bob Cudney Alexander McPherson

Macromolecular Substances

Water of crystallization

10.1006/bbrc.1995.1260

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Citations (49)

A new crystal form of bovine pancreatic RNase A in complex with 2′-deoxyguanosine-5′-monophosphate

Acta Crystallographica Section F Structural Biology and Crystallization Communications (2007)

Steven B. Larson John Day Robert Cudney Alexander McPherson

The structure of bovine pancreatic RNase A has been determined in complex with 2′-deoxyguanosine-5′-monophosphate (dGMP) at 1.33 Å resolution at room temperature in a previously unreported unit cell belonging to space group P31. There are two molecules of nucleotide per enzyme molecule, one of which lies in the active-site cleft in the productive binding mode, whilst the guanine base of the other dGMP occupies the pyrimidine-specific binding site in a nonproductive mode such that it forms hydrogen bonds to the phosphate group of the first dGMP. This is the first RNase A structure containing a guanine base in the B2 binding site. Each dGMP molecule is involved in intermolecular interactions with adjacent RNase A molecules in the lattice and the two nucleotides appear to direct the formation of the crystal lattice. Because GMP may be produced during degradation of RNA, this association could represent an inhibitor complex and thereby affect the observed enzyme kinetics.

Deoxyguanosine

Bovine pancreatic ribonuclease

10.1107/s1744309107039565

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Citations (8)

Protein Crystal Growth in Microgravity

Science (1989)

Lawrence J. DeLucas Craig D. Smith Herman W. Smith Senadhi Vijay‐Kumar Shobha E. Senadhi

The crystals of most proteins or other biological macromolecules are poorly ordered and diffract to lower resolutions than those observed for most crystals of simple organic and inorganic compounds. Crystallization in the microgravity environment of space may improve crystal quality by eliminating convection effects near growing crystal surfaces. A series of 11 different protein crystal growth experiments was performed on U.S. space shuttle flight STS-26 in September 1988. The microgravity-grown crystals of γ-interferon D 1 , porcine elastase, and isocitrate lyase are larger, display more uniform morphologies, and yield diffraction data to significantly higher resolutions than the best crystals of these proteins grown on Earth.

Protein crystallization

Crystal (programming language)

10.1126/science.2510297

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Citations (185)

X-ray Crystallographic Analysis of Pig Pancreatic Alpha-Amylase with Limit Dextrin and Oligosaccharide

S. B. Larson John Day Alexander McPherson

Dextrin

Alpha-amylase

Alpha (finance)

Oligosaccharide

10.2210/pdb3l2l/pdb

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Citations (0)