University of Alabama at Birmingham

Graduate Research Assistant

(3 years 7 months)
- Assist in design, logistics, inventory and management of experiments for a 5M NASA Crystallography in Microgravity research grant
- Purify, crystallize and solve the three-dimensional structure of identified target proteins
- Work with local high schools to teach students how to crystallize proteins for NASA's educational outreach program
- Improving the resolution of X-ray diffraction patterns of crystalized proteins by growing them in near-zero gravity by capillary diffusion and vapor diffusion on the International Space Station,
launched on SpaceX3 April 2014
- Utilizing Self Interaction Chromatography (SIC) to solubilize and crystallize membrane and aqueous proteins

Southern Research

Biologist

Derek worked at Southern Research as a Biologist

Son Shines Hope International

Board of Directors at Son Shines Hope International

- Create and review a statement of mission and purpose that articulates the organization's goals, means, and primary constituents
- Actively participate in an overall planning process and assist in implementing and
monitoring the plan's goals
- Determine which programs are consistent with the organization's mission and
monitor their effectiveness
- Secure adequate resources for the organization to fulfill its mission
- Assist in developing the annual budget and ensuring that proper financial controls are in place
- Articulate Son Shines Hope International's mission, accomplishments, and goals to the public and garner support from the community

Birmingham City Schools

IB Life Sciences Instructor 7th Grade

Derek worked at Birmingham City Schools as a IB Life Sciences Instructor 7th Grade

The University of Alabama at Birmingham

Gradaute Teaching Assistant

- Teach hands-on laboratory experiences for Introductory Biology for Majors
- Develop lectures for each topic covered
- Review experimental procedures with students prior to beginning experiments
- Assist students with experiments while teaching them how to examine biological questions by utilizing the scientific method
- Create, administer and grade all exams and practicals given to students

VIPKID

ESL Instructor

- Teach students in China how to read and speak fluent English from the comfort of their home
- Create a fun and rich learning environment that both support and encourages students to learn to read and speak English

To Join our team of teachers: https://t.vipkid.com.cn/?refereeId=6613477&refersourceid=a01
Referral code: 03XQZP

BAO (Birmingham AIDS Outreach)

Volunteer at BAO Open Houses

Hands On Birmingham

Volunteer for various clean-up activities around the city's rivers, stream and neighborhoods

1.55 Å resolution X-ray crystal structure of Rv3902c from Mycobacterium tuberculosis

Acta Crystallogr F Struct Biol

The crystallographic structure of the Mycobacterium tuberculosis (TB) protein Rv3902c (176 residues; molecular mass of 19.8 kDa) was determined at 1.55 Å resolution. The function of Rv3902c is unknown, although several TB genes involved in bacterial pathogenesis are expressed from the operon containing the Rv3902c gene. The unique structural fold of Rv3902c contains two domains, each consisting of antiparallel β-sheets and α-helices, creating a hand-like binding motif with a small binding pocket in the palm. Structural homology searches reveal that Rv3902c has an overall structure similar to that of the Salmonella virulence-factor chaperone InvB, with an r.m.s.d. for main-chain atoms of 2.3 Å along an aligned domain. Keywords: Mycobacterium tuberculosis, Rv3902c, virulence-factor chaperone, novel fold

1.55 Å resolution X-ray crystal structure of Rv3902c from Mycobacterium tuberculosis

Acta Crystallogr F Struct Biol

The crystallographic structure of the Mycobacterium tuberculosis (TB) protein Rv3902c (176 residues; molecular mass of 19.8 kDa) was determined at 1.55 Å resolution. The function of Rv3902c is unknown, although several TB genes involved in bacterial pathogenesis are expressed from the operon containing the Rv3902c gene. The unique structural fold of Rv3902c contains two domains, each consisting of antiparallel β-sheets and α-helices, creating a hand-like binding motif with a small binding pocket in the palm. Structural homology searches reveal that Rv3902c has an overall structure similar to that of the Salmonella virulence-factor chaperone InvB, with an r.m.s.d. for main-chain atoms of 2.3 Å along an aligned domain. Keywords: Mycobacterium tuberculosis, Rv3902c, virulence-factor chaperone, novel fold

1.55 Å resolution X-ray crystal structure of Rv3902c from Mycobacterium tuberculosis

Acta Crystallogr F Struct Biol

The crystallographic structure of the Mycobacterium tuberculosis (TB) protein Rv3902c (176 residues; molecular mass of 19.8 kDa) was determined at 1.55 Å resolution. The function of Rv3902c is unknown, although several TB genes involved in bacterial pathogenesis are expressed from the operon containing the Rv3902c gene. The unique structural fold of Rv3902c contains two domains, each consisting of antiparallel β-sheets and α-helices, creating a hand-like binding motif with a small binding pocket in the palm. Structural homology searches reveal that Rv3902c has an overall structure similar to that of the Salmonella virulence-factor chaperone InvB, with an r.m.s.d. for main-chain atoms of 2.3 Å along an aligned domain. Keywords: Mycobacterium tuberculosis, Rv3902c, virulence-factor chaperone, novel fold